2G50
The location of the allosteric amino acid binding site of muscle pyruvate kinase.
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0003729 | molecular_function | mRNA binding |
A | 0003824 | molecular_function | catalytic activity |
A | 0004713 | molecular_function | protein tyrosine kinase activity |
A | 0004743 | molecular_function | pyruvate kinase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005524 | molecular_function | ATP binding |
A | 0005634 | cellular_component | nucleus |
A | 0005737 | cellular_component | cytoplasm |
A | 0005791 | cellular_component | rough endoplasmic reticulum |
A | 0006096 | biological_process | glycolytic process |
A | 0006417 | biological_process | regulation of translation |
A | 0016301 | molecular_function | kinase activity |
A | 0030955 | molecular_function | potassium ion binding |
A | 0032869 | biological_process | cellular response to insulin stimulus |
A | 0046872 | molecular_function | metal ion binding |
A | 1903672 | biological_process | positive regulation of sprouting angiogenesis |
A | 2000767 | biological_process | positive regulation of cytoplasmic translation |
B | 0000287 | molecular_function | magnesium ion binding |
B | 0003729 | molecular_function | mRNA binding |
B | 0003824 | molecular_function | catalytic activity |
B | 0004713 | molecular_function | protein tyrosine kinase activity |
B | 0004743 | molecular_function | pyruvate kinase activity |
B | 0005515 | molecular_function | protein binding |
B | 0005524 | molecular_function | ATP binding |
B | 0005634 | cellular_component | nucleus |
B | 0005737 | cellular_component | cytoplasm |
B | 0005791 | cellular_component | rough endoplasmic reticulum |
B | 0006096 | biological_process | glycolytic process |
B | 0006417 | biological_process | regulation of translation |
B | 0016301 | molecular_function | kinase activity |
B | 0030955 | molecular_function | potassium ion binding |
B | 0032869 | biological_process | cellular response to insulin stimulus |
B | 0046872 | molecular_function | metal ion binding |
B | 1903672 | biological_process | positive regulation of sprouting angiogenesis |
B | 2000767 | biological_process | positive regulation of cytoplasmic translation |
C | 0000287 | molecular_function | magnesium ion binding |
C | 0003729 | molecular_function | mRNA binding |
C | 0003824 | molecular_function | catalytic activity |
C | 0004713 | molecular_function | protein tyrosine kinase activity |
C | 0004743 | molecular_function | pyruvate kinase activity |
C | 0005515 | molecular_function | protein binding |
C | 0005524 | molecular_function | ATP binding |
C | 0005634 | cellular_component | nucleus |
C | 0005737 | cellular_component | cytoplasm |
C | 0005791 | cellular_component | rough endoplasmic reticulum |
C | 0006096 | biological_process | glycolytic process |
C | 0006417 | biological_process | regulation of translation |
C | 0016301 | molecular_function | kinase activity |
C | 0030955 | molecular_function | potassium ion binding |
C | 0032869 | biological_process | cellular response to insulin stimulus |
C | 0046872 | molecular_function | metal ion binding |
C | 1903672 | biological_process | positive regulation of sprouting angiogenesis |
C | 2000767 | biological_process | positive regulation of cytoplasmic translation |
D | 0000287 | molecular_function | magnesium ion binding |
D | 0003729 | molecular_function | mRNA binding |
D | 0003824 | molecular_function | catalytic activity |
D | 0004713 | molecular_function | protein tyrosine kinase activity |
D | 0004743 | molecular_function | pyruvate kinase activity |
D | 0005515 | molecular_function | protein binding |
D | 0005524 | molecular_function | ATP binding |
D | 0005634 | cellular_component | nucleus |
D | 0005737 | cellular_component | cytoplasm |
D | 0005791 | cellular_component | rough endoplasmic reticulum |
D | 0006096 | biological_process | glycolytic process |
D | 0006417 | biological_process | regulation of translation |
D | 0016301 | molecular_function | kinase activity |
D | 0030955 | molecular_function | potassium ion binding |
D | 0032869 | biological_process | cellular response to insulin stimulus |
D | 0046872 | molecular_function | metal ion binding |
D | 1903672 | biological_process | positive regulation of sprouting angiogenesis |
D | 2000767 | biological_process | positive regulation of cytoplasmic translation |
E | 0000287 | molecular_function | magnesium ion binding |
E | 0003729 | molecular_function | mRNA binding |
E | 0003824 | molecular_function | catalytic activity |
E | 0004713 | molecular_function | protein tyrosine kinase activity |
E | 0004743 | molecular_function | pyruvate kinase activity |
E | 0005515 | molecular_function | protein binding |
E | 0005524 | molecular_function | ATP binding |
E | 0005634 | cellular_component | nucleus |
E | 0005737 | cellular_component | cytoplasm |
E | 0005791 | cellular_component | rough endoplasmic reticulum |
E | 0006096 | biological_process | glycolytic process |
E | 0006417 | biological_process | regulation of translation |
E | 0016301 | molecular_function | kinase activity |
E | 0030955 | molecular_function | potassium ion binding |
E | 0032869 | biological_process | cellular response to insulin stimulus |
E | 0046872 | molecular_function | metal ion binding |
E | 1903672 | biological_process | positive regulation of sprouting angiogenesis |
E | 2000767 | biological_process | positive regulation of cytoplasmic translation |
F | 0000287 | molecular_function | magnesium ion binding |
F | 0003729 | molecular_function | mRNA binding |
F | 0003824 | molecular_function | catalytic activity |
F | 0004713 | molecular_function | protein tyrosine kinase activity |
F | 0004743 | molecular_function | pyruvate kinase activity |
F | 0005515 | molecular_function | protein binding |
F | 0005524 | molecular_function | ATP binding |
F | 0005634 | cellular_component | nucleus |
F | 0005737 | cellular_component | cytoplasm |
F | 0005791 | cellular_component | rough endoplasmic reticulum |
F | 0006096 | biological_process | glycolytic process |
F | 0006417 | biological_process | regulation of translation |
F | 0016301 | molecular_function | kinase activity |
F | 0030955 | molecular_function | potassium ion binding |
F | 0032869 | biological_process | cellular response to insulin stimulus |
F | 0046872 | molecular_function | metal ion binding |
F | 1903672 | biological_process | positive regulation of sprouting angiogenesis |
F | 2000767 | biological_process | positive regulation of cytoplasmic translation |
G | 0000287 | molecular_function | magnesium ion binding |
G | 0003729 | molecular_function | mRNA binding |
G | 0003824 | molecular_function | catalytic activity |
G | 0004713 | molecular_function | protein tyrosine kinase activity |
G | 0004743 | molecular_function | pyruvate kinase activity |
G | 0005515 | molecular_function | protein binding |
G | 0005524 | molecular_function | ATP binding |
G | 0005634 | cellular_component | nucleus |
G | 0005737 | cellular_component | cytoplasm |
G | 0005791 | cellular_component | rough endoplasmic reticulum |
G | 0006096 | biological_process | glycolytic process |
G | 0006417 | biological_process | regulation of translation |
G | 0016301 | molecular_function | kinase activity |
G | 0030955 | molecular_function | potassium ion binding |
G | 0032869 | biological_process | cellular response to insulin stimulus |
G | 0046872 | molecular_function | metal ion binding |
G | 1903672 | biological_process | positive regulation of sprouting angiogenesis |
G | 2000767 | biological_process | positive regulation of cytoplasmic translation |
H | 0000287 | molecular_function | magnesium ion binding |
H | 0003729 | molecular_function | mRNA binding |
H | 0003824 | molecular_function | catalytic activity |
H | 0004713 | molecular_function | protein tyrosine kinase activity |
H | 0004743 | molecular_function | pyruvate kinase activity |
H | 0005515 | molecular_function | protein binding |
H | 0005524 | molecular_function | ATP binding |
H | 0005634 | cellular_component | nucleus |
H | 0005737 | cellular_component | cytoplasm |
H | 0005791 | cellular_component | rough endoplasmic reticulum |
H | 0006096 | biological_process | glycolytic process |
H | 0006417 | biological_process | regulation of translation |
H | 0016301 | molecular_function | kinase activity |
H | 0030955 | molecular_function | potassium ion binding |
H | 0032869 | biological_process | cellular response to insulin stimulus |
H | 0046872 | molecular_function | metal ion binding |
H | 1903672 | biological_process | positive regulation of sprouting angiogenesis |
H | 2000767 | biological_process | positive regulation of cytoplasmic translation |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MN A 640 |
Chain | Residue |
A | GLU271 |
A | ASP295 |
A | PYR600 |
A | HOH6777 |
A | HOH6778 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE K A 6501 |
Chain | Residue |
A | HOH6776 |
A | HOH6779 |
A | ASN74 |
A | SER76 |
A | ASP112 |
A | THR113 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MN B 640 |
Chain | Residue |
B | GLU271 |
B | ASP295 |
B | PYR600 |
B | HOH6929 |
B | HOH6930 |
site_id | AC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE K B 6502 |
Chain | Residue |
B | ASN74 |
B | SER76 |
B | ASP112 |
B | THR113 |
B | SER242 |
B | HOH6928 |
B | HOH6931 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MN C 640 |
Chain | Residue |
C | GLU271 |
C | ASP295 |
C | PYR600 |
C | HOH6693 |
C | HOH6694 |
site_id | AC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE K C 6503 |
Chain | Residue |
C | ASN74 |
C | SER76 |
C | ASP112 |
C | THR113 |
C | SER242 |
C | HOH6692 |
C | HOH6695 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MN D 640 |
Chain | Residue |
D | GLU271 |
D | ASP295 |
D | PYR600 |
D | HOH7070 |
D | HOH7073 |
site_id | AC8 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE K D 6504 |
Chain | Residue |
D | ASN74 |
D | SER76 |
D | ASP112 |
D | THR113 |
D | SER242 |
D | HOH7071 |
D | HOH7072 |
site_id | AC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MN E 640 |
Chain | Residue |
E | GLU271 |
E | ASP295 |
E | PYR600 |
E | HOH3432 |
E | HOH3433 |
site_id | BC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE K E 6505 |
Chain | Residue |
E | ASN74 |
E | SER76 |
E | ASP112 |
E | THR113 |
E | HOH3431 |
E | HOH3434 |
site_id | BC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MN F 640 |
Chain | Residue |
F | GLU271 |
F | ASP295 |
F | PYR600 |
F | HOH6523 |
F | HOH6825 |
site_id | BC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE K F 6506 |
Chain | Residue |
F | ASN74 |
F | SER76 |
F | ASP112 |
F | THR113 |
F | SER242 |
F | HOH6524 |
F | HOH6824 |
site_id | BC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MN G 640 |
Chain | Residue |
G | GLU271 |
G | ASP295 |
G | PYR600 |
G | HOH2776 |
G | HOH2777 |
site_id | BC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE K G 6507 |
Chain | Residue |
G | ASN74 |
G | SER76 |
G | ASP112 |
G | THR113 |
G | SER242 |
G | HOH2775 |
G | HOH2778 |
site_id | BC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MN H 640 |
Chain | Residue |
H | GLU271 |
H | ASP295 |
H | PYR600 |
H | HOH6673 |
H | HOH6674 |
site_id | BC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE K H 6508 |
Chain | Residue |
H | ASN74 |
H | SER76 |
H | ASP112 |
H | THR113 |
H | HOH6672 |
H | HOH6675 |
site_id | BC8 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE NA A 6019 |
Chain | Residue |
A | HOH7007 |
A | LYS124 |
A | GLY125 |
A | SER126 |
A | GLY127 |
A | THR128 |
A | HOH7006 |
site_id | BC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NA D 6020 |
Chain | Residue |
D | LYS124 |
D | GLY125 |
D | SER126 |
D | GLY127 |
D | THR128 |
D | HOH6753 |
site_id | CC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NA E 6021 |
Chain | Residue |
E | LYS124 |
E | GLY125 |
E | SER126 |
E | GLY127 |
E | THR128 |
E | HOH4539 |
site_id | CC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE NA H 6022 |
Chain | Residue |
H | LYS124 |
H | GLY125 |
H | SER126 |
H | GLY127 |
H | THR128 |
H | HOH6510 |
H | HOH6745 |
site_id | CC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE NA A 6023 |
Chain | Residue |
A | THR431 |
A | SER436 |
A | HOH6812 |
site_id | CC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE NA B 6024 |
Chain | Residue |
B | THR431 |
B | SER436 |
B | HOH6556 |
site_id | CC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE NA C 6025 |
Chain | Residue |
C | THR431 |
C | SER436 |
C | HOH6628 |
site_id | CC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE NA D 6026 |
Chain | Residue |
D | THR431 |
D | SER436 |
D | HOH6516 |
site_id | CC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE NA F 6027 |
Chain | Residue |
F | THR431 |
F | SER436 |
F | HOH6754 |
site_id | CC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE NA G 6028 |
Chain | Residue |
G | THR431 |
G | SER436 |
G | HOH3003 |
site_id | CC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE NA H 6029 |
Chain | Residue |
H | THR431 |
H | SER436 |
H | HOH6625 |
site_id | DC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE NA E 6030 |
Chain | Residue |
E | THR431 |
E | SER436 |
E | HOH4160 |
site_id | DC2 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE ALA A 6101 |
Chain | Residue |
A | ARG42 |
A | ASN43 |
A | ASN69 |
A | ARG105 |
A | HIS463 |
A | ILE468 |
A | PHE469 |
A | PRO470 |
A | HOH6548 |
A | HOH6549 |
A | HOH7059 |
site_id | DC3 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE PYR A 600 |
Chain | Residue |
A | LYS269 |
A | GLU271 |
A | ALA292 |
A | ARG293 |
A | GLY294 |
A | ASP295 |
A | THR327 |
A | MN640 |
A | HOH6776 |
A | HOH6777 |
A | HOH6778 |
site_id | DC4 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE ALA B 6102 |
Chain | Residue |
B | ARG42 |
B | ASN43 |
B | ASN69 |
B | HIS463 |
B | ILE468 |
B | PHE469 |
B | PRO470 |
B | EDO6032 |
B | HOH6758 |
B | HOH6765 |
B | HOH6766 |
site_id | DC5 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE PYR B 600 |
Chain | Residue |
B | LYS269 |
B | GLU271 |
B | ALA292 |
B | ARG293 |
B | GLY294 |
B | ASP295 |
B | THR327 |
B | MN640 |
B | HOH6928 |
B | HOH6929 |
B | HOH6930 |
site_id | DC6 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE ALA C 6103 |
Chain | Residue |
C | ARG42 |
C | ASN43 |
C | ASN69 |
C | ARG105 |
C | HIS463 |
C | ILE468 |
C | PHE469 |
C | PRO470 |
C | HOH6535 |
C | HOH6547 |
C | HOH7053 |
site_id | DC7 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE PYR C 600 |
Chain | Residue |
C | LYS269 |
C | GLU271 |
C | ALA292 |
C | ARG293 |
C | GLY294 |
C | ASP295 |
C | THR327 |
C | MN640 |
C | HOH6692 |
C | HOH6693 |
C | HOH6694 |
site_id | DC8 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE ALA D 6104 |
Chain | Residue |
D | ARG42 |
D | ASN43 |
D | ASN69 |
D | ARG105 |
D | HIS463 |
D | ILE468 |
D | PHE469 |
D | PRO470 |
D | HOH6995 |
D | HOH6998 |
D | HOH7124 |
site_id | DC9 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE PYR D 600 |
Chain | Residue |
D | LYS269 |
D | GLU271 |
D | ALA292 |
D | ARG293 |
D | GLY294 |
D | ASP295 |
D | THR327 |
D | MN640 |
D | EDO6033 |
D | HOH7070 |
D | HOH7072 |
D | HOH7073 |
site_id | EC1 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE ALA E 6105 |
Chain | Residue |
E | ARG42 |
E | ASN43 |
E | ASN69 |
E | ARG105 |
E | HIS463 |
E | ILE468 |
E | PHE469 |
E | PRO470 |
E | HOH3633 |
E | HOH3634 |
E | HOH4515 |
E | HOH4823 |
site_id | EC2 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE PYR E 600 |
Chain | Residue |
E | LYS269 |
E | GLU271 |
E | ALA292 |
E | ARG293 |
E | GLY294 |
E | ASP295 |
E | THR327 |
E | MN640 |
E | HOH3431 |
E | HOH3432 |
E | HOH3433 |
site_id | EC3 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE ALA F 6106 |
Chain | Residue |
F | ARG42 |
F | ASN43 |
F | ASN69 |
F | ARG105 |
F | HIS463 |
F | ILE468 |
F | PHE469 |
F | PRO470 |
F | HOH6646 |
F | HOH6647 |
F | HOH7014 |
site_id | EC4 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE PYR F 600 |
Chain | Residue |
F | LYS269 |
F | GLU271 |
F | ALA292 |
F | ARG293 |
F | GLY294 |
F | ASP295 |
F | THR327 |
F | MN640 |
F | GOL6057 |
F | HOH6523 |
F | HOH6524 |
F | HOH6825 |
site_id | EC5 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE ALA G 6107 |
Chain | Residue |
G | ARG42 |
G | ASN43 |
G | ASN69 |
G | ARG105 |
G | HIS463 |
G | ILE468 |
G | PHE469 |
G | PRO470 |
G | HOH3727 |
G | HOH3728 |
G | HOH4510 |
site_id | EC6 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE PYR G 600 |
Chain | Residue |
G | LYS269 |
G | GLU271 |
G | ALA292 |
G | ARG293 |
G | GLY294 |
G | ASP295 |
G | THR327 |
G | MN640 |
G | HOH2775 |
G | HOH2776 |
G | HOH2777 |
site_id | EC7 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE ALA H 6108 |
Chain | Residue |
H | ARG42 |
H | ASN43 |
H | ASN69 |
H | ARG105 |
H | HIS463 |
H | ILE468 |
H | PHE469 |
H | PRO470 |
H | HOH6893 |
H | HOH6894 |
H | HOH6960 |
site_id | EC8 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE PYR H 600 |
Chain | Residue |
H | LYS269 |
H | GLU271 |
H | ALA292 |
H | ARG293 |
H | GLY294 |
H | ASP295 |
H | THR327 |
H | MN640 |
H | EDO6041 |
H | HOH6672 |
H | HOH6673 |
H | HOH6674 |
site_id | EC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO D 6011 |
Chain | Residue |
D | PRO38 |
D | THR40 |
D | HOH6618 |
site_id | FC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO F 6012 |
Chain | Residue |
F | PRO38 |
F | THR40 |
F | HOH6631 |
F | HOH6637 |
site_id | FC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO B 6013 |
Chain | Residue |
B | PRO38 |
B | THR40 |
B | HOH6977 |
site_id | FC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO C 6014 |
Chain | Residue |
C | PRO38 |
C | THR40 |
C | HOH6573 |
site_id | FC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO E 6015 |
Chain | Residue |
E | PRO38 |
E | THR40 |
G | EDO6016 |
site_id | FC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO G 6016 |
Chain | Residue |
E | ALA37 |
E | EDO6015 |
G | LYS304 |
G | HOH2692 |
site_id | FC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO D 6017 |
Chain | Residue |
D | ARG72 |
D | ASN74 |
D | SER361 |
D | GLY362 |
D | HOH6676 |
D | HOH7072 |
site_id | FC7 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE EDO B 6032 |
Chain | Residue |
B | TYR104 |
B | ARG105 |
B | PRO106 |
B | HIS463 |
B | PHE469 |
B | PRO470 |
B | ARG499 |
B | ALA6102 |
B | HOH6755 |
B | HOH6758 |
site_id | FC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO D 6033 |
Chain | Residue |
D | ASP177 |
D | GLY294 |
D | PYR600 |
site_id | FC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO H 6034 |
Chain | Residue |
H | ARG72 |
H | ASN74 |
H | SER361 |
H | HOH6667 |
H | HOH6668 |
H | HOH6772 |
site_id | GC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO F 6036 |
Chain | Residue |
F | ARG338 |
F | PRO339 |
F | ARG341 |
F | HOH6514 |
H | ASP177 |
H | GLN328 |
site_id | GC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO H 6037 |
Chain | Residue |
H | GLU284 |
H | ALA285 |
H | SER286 |
H | ASP287 |
H | LYS321 |
H | HOH6709 |
H | HOH7085 |
site_id | GC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO E 6038 |
Chain | Residue |
E | ARG72 |
E | ASN74 |
E | SER361 |
E | GLY362 |
E | HOH3429 |
E | EDO6046 |
site_id | GC4 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE EDO E 6039 |
Chain | Residue |
E | ASP177 |
site_id | GC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO D 6040 |
Chain | Residue |
D | THR138 |
D | GLU153 |
D | ASN154 |
site_id | GC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO H 6041 |
Chain | Residue |
H | ASP177 |
H | GLY294 |
H | ASP295 |
H | PYR600 |
H | HOH6525 |
site_id | GC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO H 6042 |
Chain | Residue |
F | ARG318 |
H | GLU27 |
H | CYS30 |
H | HOH7076 |
site_id | GC8 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO A 6043 |
Chain | Residue |
A | GLU95 |
A | TYR104 |
A | HIS456 |
A | ARG460 |
A | HOH6559 |
A | HOH6698 |
A | HOH6701 |
A | HOH7111 |
site_id | GC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO C 6044 |
Chain | Residue |
A | ASP177 |
A | GLN328 |
C | PRO339 |
C | ARG341 |
C | HOH7078 |
site_id | HC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO E 6045 |
Chain | Residue |
E | ARG55 |
E | TYR82 |
E | HOH2717 |
E | HOH5069 |
E | GOL6031 |
H | HOH6567 |
site_id | HC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO E 6046 |
Chain | Residue |
E | ILE50 |
E | GLY51 |
E | ASN74 |
E | ALA365 |
E | LYS366 |
E | HOH3458 |
E | EDO6038 |
site_id | HC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO B 6047 |
Chain | Residue |
B | ARG254 |
B | GLU284 |
B | ALA285 |
B | SER286 |
B | ASP287 |
B | LYS321 |
B | HOH6897 |
B | HOH7013 |
site_id | HC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO B 6048 |
Chain | Residue |
B | ASP177 |
B | GLY294 |
B | ASP295 |
B | GOL6302 |
B | HOH6922 |
B | HOH6924 |
B | HOH7001 |
B | HOH7009 |
site_id | HC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO E 6049 |
Chain | Residue |
E | GLU284 |
E | ALA285 |
E | SER286 |
E | LYS321 |
E | HOH3355 |
E | HOH4836 |
E | HOH4961 |
site_id | HC6 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO A 6050 |
Chain | Residue |
A | GLU284 |
A | ALA285 |
A | SER286 |
A | ASP287 |
A | LYS321 |
A | HOH7107 |
A | HOH7115 |
A | HOH7120 |
site_id | HC7 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO A 6051 |
Chain | Residue |
A | ARG338 |
A | PRO339 |
A | THR340 |
A | ARG341 |
A | HOH7048 |
C | ASP177 |
C | LEU179 |
C | GLN328 |
site_id | HC8 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO G 6052 |
Chain | Residue |
G | ARG42 |
G | LYS65 |
G | SER66 |
G | GLY67 |
G | HOH3479 |
G | HOH3726 |
G | HOH3729 |
site_id | HC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO H 6053 |
Chain | Residue |
H | GLU58 |
H | LYS61 |
H | HOH6652 |
site_id | IC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO H 6054 |
Chain | Residue |
E | GOL6031 |
H | PRO52 |
H | ALA53 |
H | SER54 |
H | ARG55 |
H | SER56 |
H | THR59 |
H | HOH6660 |
site_id | IC2 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE ETE B 6018 |
Chain | Residue |
B | THR49 |
B | ILE50 |
B | GLY51 |
B | PRO52 |
B | ARG72 |
B | ASN74 |
B | ALA365 |
B | LYS366 |
B | HOH6655 |
B | HOH6928 |
B | HOH6954 |
B | HOH7011 |
site_id | IC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL A 6201 |
Chain | Residue |
A | PRO116 |
A | ASN209 |
A | LEU210 |
A | VAL215 |
A | ARG245 |
A | GLU299 |
A | HOH6657 |
A | HOH6658 |
site_id | IC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL A 6301 |
Chain | Residue |
A | GLU117 |
A | ILE118 |
A | GLY207 |
A | VAL208 |
A | PHE243 |
A | ASP295 |
A | HOH6755 |
A | HOH6777 |
site_id | IC5 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL B 6202 |
Chain | Residue |
B | PRO116 |
B | ASN209 |
B | LEU210 |
B | VAL215 |
B | ARG245 |
B | GLU299 |
B | HOH6613 |
B | HOH6614 |
B | HOH6615 |
site_id | IC6 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL B 6302 |
Chain | Residue |
B | GLU117 |
B | ILE118 |
B | GLY207 |
B | VAL208 |
B | PHE243 |
B | ASP295 |
B | EDO6048 |
B | HOH6924 |
B | HOH6929 |
site_id | IC7 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL C 6203 |
Chain | Residue |
C | PRO116 |
C | VAL208 |
C | ASN209 |
C | LEU210 |
C | VAL215 |
C | ARG245 |
C | GLU299 |
C | HOH6865 |
site_id | IC8 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL C 6303 |
Chain | Residue |
C | GLU117 |
C | ILE118 |
C | GLY207 |
C | VAL208 |
C | PHE243 |
C | ASP295 |
C | HOH6693 |
site_id | IC9 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL D 6204 |
Chain | Residue |
D | PRO116 |
D | ASN209 |
D | LEU210 |
D | VAL215 |
D | ARG245 |
D | GLU299 |
D | HOH6876 |
D | HOH7068 |
site_id | JC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL D 6304 |
Chain | Residue |
D | GLU117 |
D | ILE118 |
D | GLY207 |
D | VAL208 |
D | PHE243 |
D | ASP295 |
D | HOH6810 |
D | HOH7073 |
site_id | JC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL E 6205 |
Chain | Residue |
E | PRO116 |
E | ASN209 |
E | LEU210 |
E | VAL215 |
E | ARG245 |
E | GLU299 |
E | HOH3598 |
E | HOH3601 |
site_id | JC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL E 6305 |
Chain | Residue |
E | GLU117 |
E | ILE118 |
E | GLY207 |
E | VAL208 |
E | PHE243 |
E | ASP295 |
E | HOH3432 |
site_id | JC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL F 6206 |
Chain | Residue |
F | PRO116 |
F | VAL208 |
F | ASN209 |
F | LEU210 |
F | VAL215 |
F | ARG245 |
F | GLU299 |
F | HOH6927 |
site_id | JC5 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL F 6306 |
Chain | Residue |
F | GLU117 |
F | ILE118 |
F | GLY207 |
F | VAL208 |
F | PHE243 |
F | ASP295 |
F | GOL6057 |
F | HOH6523 |
F | HOH6679 |
site_id | JC6 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE GOL G 6207 |
Chain | Residue |
G | PRO116 |
G | VAL208 |
G | ASN209 |
G | LEU210 |
G | VAL215 |
G | ARG245 |
G | GLU299 |
G | HOH4188 |
G | HOH4189 |
G | GOL6307 |
site_id | JC7 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL G 6307 |
Chain | Residue |
G | GLU117 |
G | ILE118 |
G | GLY207 |
G | VAL208 |
G | PHE243 |
G | ASP295 |
G | HOH2776 |
G | GOL6207 |
site_id | JC8 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL H 6208 |
Chain | Residue |
H | PRO116 |
H | ASN209 |
H | LEU210 |
H | VAL215 |
H | ARG245 |
H | GLU299 |
H | HOH7028 |
H | HOH7059 |
H | HOH7103 |
site_id | JC9 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL H 6308 |
Chain | Residue |
H | GLU117 |
H | ILE118 |
H | GLY207 |
H | VAL208 |
H | PHE243 |
H | ASP295 |
H | HOH6673 |
site_id | KC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL F 6001 |
Chain | Residue |
F | LYS229 |
F | GLU233 |
F | ILE256 |
F | LEU257 |
F | LYS260 |
F | HOH6610 |
F | HOH6611 |
site_id | KC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL A 6002 |
Chain | Residue |
A | ARG42 |
A | LYS65 |
A | SER66 |
A | GLY67 |
A | HIS378 |
A | HOH6844 |
A | HOH7129 |
A | HOH7141 |
site_id | KC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL G 6004 |
Chain | Residue |
G | ALA37 |
G | PRO38 |
G | ILE39 |
G | THR40 |
G | ARG382 |
G | HOH3521 |
G | HOH3733 |
site_id | KC4 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL F 6005 |
Chain | Residue |
F | ARG42 |
F | LYS65 |
F | SER66 |
F | GLY67 |
F | HIS378 |
F | HOH6638 |
F | HOH6642 |
F | HOH7067 |
F | HOH7071 |
site_id | KC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL H 6006 |
Chain | Residue |
H | ILE64 |
H | PHE97 |
H | LEU103 |
H | ARG105 |
H | ARG499 |
H | HOH6896 |
H | HOH6963 |
site_id | KC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL B 6007 |
Chain | Residue |
B | ARG42 |
B | LYS65 |
B | SER66 |
B | GLY67 |
B | HIS378 |
B | HOH6757 |
B | HOH6762 |
site_id | KC7 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL H 6008 |
Chain | Residue |
H | ARG42 |
H | LYS65 |
H | SER66 |
H | GLY67 |
H | HIS378 |
H | HOH6551 |
H | HOH6895 |
H | HOH7069 |
site_id | KC8 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL F 6010 |
Chain | Residue |
F | ASP177 |
F | GLN328 |
F | HOH6677 |
F | HOH7070 |
H | ARG338 |
H | PRO339 |
H | ARG341 |
H | HOH6777 |
site_id | KC9 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE GOL E 6031 |
Chain | Residue |
E | PRO52 |
E | HOH2717 |
E | HOH2718 |
E | HOH4678 |
E | HOH4816 |
E | EDO6045 |
H | PRO52 |
H | ARG55 |
H | TYR82 |
H | EDO6054 |
H | HOH6661 |
site_id | LC1 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE GOL C 6055 |
Chain | Residue |
C | ILE64 |
C | PHE97 |
C | LEU103 |
C | TYR104 |
C | ARG105 |
C | ARG499 |
C | HOH6538 |
C | HOH6540 |
C | HOH6778 |
C | HOH6946 |
site_id | LC2 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL C 6056 |
Chain | Residue |
C | GLU417 |
C | TYR420 |
C | LYS421 |
C | HOH6582 |
C | HOH6584 |
C | HOH7019 |
C | HOH7054 |
D | ALA398 |
D | HOH7028 |
site_id | LC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL F 6057 |
Chain | Residue |
F | ASP177 |
F | GLY294 |
F | ASP295 |
F | ILE298 |
F | PYR600 |
F | GOL6306 |
F | HOH6523 |
Functional Information from PROSITE/UniProt
site_id | PS00110 |
Number of Residues | 13 |
Details | PYRUVATE_KINASE Pyruvate kinase active site signature. IkIISKIENhEGV |
Chain | Residue | Details |
A | ILE264-VAL276 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 112 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P14618 |
Chain | Residue | Details |
A | ASN272 | |
A | GLU432 | |
A | LEU464 | |
A | ALA482 | |
A | VAL489 | |
A | PRO516 | |
B | VAL70 | |
B | PHE75 | |
B | HIS77 | |
B | PRO106 | |
B | THR113 | |
B | LYS114 | |
B | THR120 | |
B | GLY207 | |
B | ASN272 | |
B | GLU432 | |
B | LEU464 | |
B | ALA482 | |
B | VAL489 | |
B | PRO516 | |
C | VAL70 | |
C | PHE75 | |
C | HIS77 | |
C | PRO106 | |
C | THR113 | |
C | LYS114 | |
C | THR120 | |
C | GLY207 | |
C | ASN272 | |
C | GLU432 | |
C | LEU464 | |
C | ALA482 | |
C | VAL489 | |
C | PRO516 | |
D | VAL70 | |
D | PHE75 | |
D | HIS77 | |
D | PRO106 | |
D | THR113 | |
D | LYS114 | |
D | THR120 | |
D | GLY207 | |
D | ASN272 | |
D | GLU432 | |
D | LEU464 | |
D | ALA482 | |
D | VAL489 | |
D | PRO516 | |
E | VAL70 | |
E | PHE75 | |
E | HIS77 | |
E | PRO106 | |
E | THR113 | |
E | LYS114 | |
E | THR120 | |
E | GLY207 | |
E | ASN272 | |
E | GLU432 | |
E | LEU464 | |
E | ALA482 | |
E | VAL489 | |
E | PRO516 | |
F | VAL70 | |
F | PHE75 | |
F | HIS77 | |
F | PRO106 | |
F | THR113 | |
F | LYS114 | |
F | THR120 | |
F | GLY207 | |
F | ASN272 | |
F | GLU432 | |
F | LEU464 | |
F | ALA482 | |
F | VAL489 | |
F | PRO516 | |
G | VAL70 | |
G | PHE75 | |
G | HIS77 | |
G | PRO106 | |
G | THR113 | |
G | LYS114 | |
G | THR120 | |
G | GLY207 | |
G | ASN272 | |
G | GLU432 | |
G | LEU464 | |
G | ALA482 | |
G | VAL489 | |
G | PRO516 | |
H | VAL70 | |
H | PHE75 | |
H | HIS77 | |
H | PRO106 | |
H | THR113 | |
H | LYS114 | |
H | THR120 | |
H | GLY207 | |
H | ASN272 | |
H | GLU432 | |
H | LEU464 | |
H | ALA482 | |
H | VAL489 | |
H | PRO516 | |
A | VAL70 | |
A | PHE75 | |
A | HIS77 | |
A | PRO106 | |
A | THR113 | |
A | LYS114 | |
A | THR120 | |
A | GLY207 |
site_id | SWS_FT_FI2 |
Number of Residues | 40 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P30613 |
Chain | Residue | Details |
E | GLN328 | |
F | MET73 | |
F | ILE270 | |
F | ASP295 | |
F | LEU296 | |
F | GLN328 | |
G | MET73 | |
G | ILE270 | |
G | ASP295 | |
G | LEU296 | |
G | GLN328 | |
H | MET73 | |
H | ILE270 | |
H | ASP295 | |
H | LEU296 | |
H | GLN328 | |
A | MET73 | |
A | ILE270 | |
A | ASP295 | |
A | LEU296 | |
A | GLN328 | |
B | MET73 | |
B | ILE270 | |
B | ASP295 | |
B | LEU296 | |
B | GLN328 | |
C | MET73 | |
C | ILE270 | |
C | ASP295 | |
C | LEU296 | |
C | GLN328 | |
D | MET73 | |
D | ILE270 | |
D | ASP295 | |
D | LEU296 | |
D | GLN328 | |
E | MET73 | |
E | ILE270 | |
E | ASP295 | |
E | LEU296 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | SITE: Transition state stabilizer => ECO:0000250|UniProtKB:P00549 |
Chain | Residue | Details |
A | ILE270 | |
B | ILE270 | |
C | ILE270 | |
D | ILE270 | |
E | ILE270 | |
F | ILE270 | |
G | ILE270 | |
H | ILE270 |
site_id | SWS_FT_FI4 |
Number of Residues | 8 |
Details | MOD_RES: N-acetylserine => ECO:0000250|UniProtKB:P11979 |
Chain | Residue | Details |
A | LYS2 | |
B | LYS2 | |
C | LYS2 | |
D | LYS2 | |
E | LYS2 | |
F | LYS2 | |
G | LYS2 | |
H | LYS2 |
site_id | SWS_FT_FI5 |
Number of Residues | 8 |
Details | MOD_RES: N6,N6,N6-trimethyllysine => ECO:0000250|UniProtKB:P14618 |
Chain | Residue | Details |
A | SER3 | |
B | SER3 | |
C | SER3 | |
D | SER3 | |
E | SER3 | |
F | SER3 | |
G | SER3 | |
H | SER3 |
site_id | SWS_FT_FI6 |
Number of Residues | 16 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P14618 |
Chain | Residue | Details |
A | ALA37 | |
A | GLY127 | |
B | ALA37 | |
B | GLY127 | |
C | ALA37 | |
C | GLY127 | |
D | ALA37 | |
D | GLY127 | |
E | ALA37 | |
E | GLY127 | |
F | ALA37 | |
F | GLY127 | |
G | ALA37 | |
G | GLY127 | |
H | ALA37 | |
H | GLY127 |
site_id | SWS_FT_FI7 |
Number of Residues | 16 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P14618 |
Chain | Residue | Details |
A | ALA41 | |
A | GLU195 | |
B | ALA41 | |
B | GLU195 | |
C | ALA41 | |
C | GLU195 | |
D | ALA41 | |
D | GLU195 | |
E | ALA41 | |
E | GLU195 | |
F | ALA41 | |
F | GLU195 | |
G | ALA41 | |
G | GLU195 | |
H | ALA41 | |
H | GLU195 |
site_id | SWS_FT_FI8 |
Number of Residues | 24 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P14618 |
Chain | Residue | Details |
A | GLU62 | |
A | ASN89 | |
A | VAL305 | |
B | GLU62 | |
B | ASN89 | |
B | VAL305 | |
C | GLU62 | |
C | ASN89 | |
C | VAL305 | |
D | GLU62 | |
D | ASN89 | |
D | VAL305 | |
E | GLU62 | |
E | ASN89 | |
E | VAL305 | |
F | GLU62 | |
F | ASN89 | |
F | VAL305 | |
G | GLU62 | |
G | ASN89 | |
G | VAL305 | |
H | GLU62 | |
H | ASN89 | |
H | VAL305 |
site_id | SWS_FT_FI9 |
Number of Residues | 16 |
Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P52480 |
Chain | Residue | Details |
A | SER66 | |
A | ALA498 | |
B | SER66 | |
B | ALA498 | |
C | SER66 | |
C | ALA498 | |
D | SER66 | |
D | ALA498 | |
E | SER66 | |
E | ALA498 | |
F | SER66 | |
F | ALA498 | |
G | SER66 | |
G | ALA498 | |
H | SER66 | |
H | ALA498 |
site_id | SWS_FT_FI10 |
Number of Residues | 16 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P11980 |
Chain | Residue | Details |
E | PHE97 | |
E | ASP100 | |
F | PHE97 | |
F | ASP100 | |
G | PHE97 | |
G | ASP100 | |
H | PHE97 | |
H | ASP100 | |
A | PHE97 | |
A | ASP100 | |
B | PHE97 | |
B | ASP100 | |
C | PHE97 | |
C | ASP100 | |
D | PHE97 | |
D | ASP100 |
site_id | SWS_FT_FI11 |
Number of Residues | 16 |
Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P14618 |
Chain | Residue | Details |
E | ARG105 | |
E | VAL175 | |
F | ARG105 | |
F | VAL175 | |
G | ARG105 | |
G | VAL175 | |
H | ARG105 | |
H | VAL175 | |
A | ARG105 | |
A | VAL175 | |
B | ARG105 | |
B | VAL175 | |
C | ARG105 | |
C | VAL175 | |
D | ARG105 | |
D | VAL175 |
site_id | SWS_FT_FI12 |
Number of Residues | 8 |
Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P52480 |
Chain | Residue | Details |
A | MET148 | |
B | MET148 | |
C | MET148 | |
D | MET148 | |
E | MET148 | |
F | MET148 | |
G | MET148 | |
H | MET148 |
site_id | SWS_FT_FI13 |
Number of Residues | 16 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P52480 |
Chain | Residue | Details |
A | VAL166 | |
A | PRO322 | |
B | VAL166 | |
B | PRO322 | |
C | VAL166 | |
C | PRO322 | |
D | VAL166 | |
D | PRO322 | |
E | VAL166 | |
E | PRO322 | |
F | VAL166 | |
F | PRO322 | |
G | VAL166 | |
G | PRO322 | |
H | VAL166 | |
H | PRO322 |
site_id | SWS_FT_FI14 |
Number of Residues | 8 |
Details | MOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P14618 |
Chain | Residue | Details |
A | ILE266 | |
B | ILE266 | |
C | ILE266 | |
D | ILE266 | |
E | ILE266 | |
F | ILE266 | |
G | ILE266 | |
H | ILE266 |
site_id | SWS_FT_FI15 |
Number of Residues | 8 |
Details | MOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P52480 |
Chain | Residue | Details |
A | ILE270 | |
B | ILE270 | |
C | ILE270 | |
D | ILE270 | |
E | ILE270 | |
F | ILE270 | |
G | ILE270 | |
H | ILE270 |
site_id | SWS_FT_FI16 |
Number of Residues | 8 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P52480 |
Chain | Residue | Details |
A | ASP475 | |
B | ASP475 | |
C | ASP475 | |
D | ASP475 | |
E | ASP475 | |
F | ASP475 | |
G | ASP475 | |
H | ASP475 |
site_id | SWS_FT_FI17 |
Number of Residues | 8 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0000250|UniProtKB:P14618 |
Chain | Residue | Details |
A | GLY115 | |
B | GLY115 | |
C | GLY115 | |
D | GLY115 | |
E | GLY115 | |
F | GLY115 | |
G | GLY115 | |
H | GLY115 |
site_id | SWS_FT_FI18 |
Number of Residues | 24 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0000250|UniProtKB:P14618 |
Chain | Residue | Details |
F | ILE266 | |
F | ILE270 | |
G | ILE266 | |
G | ILE270 | |
H | ILE266 | |
H | ILE270 | |
A | ILE266 | |
A | ILE270 | |
B | ILE266 | |
B | ILE270 | |
C | ILE266 | |
C | ILE270 | |
D | ILE266 | |
D | ILE270 | |
E | ILE266 | |
E | ILE270 |
site_id | SWS_FT_FI19 |
Number of Residues | 8 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate => ECO:0000250|UniProtKB:P14618 |
Chain | Residue | Details |
A | VAL166 | |
B | VAL166 | |
C | VAL166 | |
D | VAL166 | |
E | VAL166 | |
F | VAL166 | |
G | VAL166 | |
H | VAL166 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 4 |
Details | M-CSA 326 |
Chain | Residue | Details |
A | MET73 | attractive charge-charge interaction, electrostatic stabiliser, steric role |
A | THR120 | attractive charge-charge interaction, electrostatic stabiliser, steric role |
A | ILE270 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, steric role |
A | GLN328 | electrostatic stabiliser, hydrogen bond donor, increase acidity |
site_id | MCSA2 |
Number of Residues | 4 |
Details | M-CSA 326 |
Chain | Residue | Details |
B | MET73 | attractive charge-charge interaction, electrostatic stabiliser, steric role |
B | THR120 | attractive charge-charge interaction, electrostatic stabiliser, steric role |
B | ILE270 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, steric role |
B | GLN328 | electrostatic stabiliser, hydrogen bond donor, increase acidity |
site_id | MCSA3 |
Number of Residues | 4 |
Details | M-CSA 326 |
Chain | Residue | Details |
C | MET73 | attractive charge-charge interaction, electrostatic stabiliser, steric role |
C | THR120 | attractive charge-charge interaction, electrostatic stabiliser, steric role |
C | ILE270 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, steric role |
C | GLN328 | electrostatic stabiliser, hydrogen bond donor, increase acidity |
site_id | MCSA4 |
Number of Residues | 4 |
Details | M-CSA 326 |
Chain | Residue | Details |
D | MET73 | attractive charge-charge interaction, electrostatic stabiliser, steric role |
D | THR120 | attractive charge-charge interaction, electrostatic stabiliser, steric role |
D | ILE270 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, steric role |
D | GLN328 | electrostatic stabiliser, hydrogen bond donor, increase acidity |
site_id | MCSA5 |
Number of Residues | 4 |
Details | M-CSA 326 |
Chain | Residue | Details |
E | MET73 | attractive charge-charge interaction, electrostatic stabiliser, steric role |
E | THR120 | attractive charge-charge interaction, electrostatic stabiliser, steric role |
E | ILE270 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, steric role |
E | GLN328 | electrostatic stabiliser, hydrogen bond donor, increase acidity |
site_id | MCSA6 |
Number of Residues | 4 |
Details | M-CSA 326 |
Chain | Residue | Details |
F | MET73 | attractive charge-charge interaction, electrostatic stabiliser, steric role |
F | THR120 | attractive charge-charge interaction, electrostatic stabiliser, steric role |
F | ILE270 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, steric role |
F | GLN328 | electrostatic stabiliser, hydrogen bond donor, increase acidity |
site_id | MCSA7 |
Number of Residues | 4 |
Details | M-CSA 326 |
Chain | Residue | Details |
G | MET73 | attractive charge-charge interaction, electrostatic stabiliser, steric role |
G | THR120 | attractive charge-charge interaction, electrostatic stabiliser, steric role |
G | ILE270 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, steric role |
G | GLN328 | electrostatic stabiliser, hydrogen bond donor, increase acidity |
site_id | MCSA8 |
Number of Residues | 4 |
Details | M-CSA 326 |
Chain | Residue | Details |
H | MET73 | attractive charge-charge interaction, electrostatic stabiliser, steric role |
H | THR120 | attractive charge-charge interaction, electrostatic stabiliser, steric role |
H | ILE270 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, steric role |
H | GLN328 | electrostatic stabiliser, hydrogen bond donor, increase acidity |