1AQF
PYRUVATE KINASE FROM RABBIT MUSCLE WITH MG, K, AND L-PHOSPHOLACTATE
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 | 0016310 | biological_process | phosphorylation |
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 | 0016310 | biological_process | phosphorylation |
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 | 0016310 | biological_process | phosphorylation |
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 | 0016310 | biological_process | phosphorylation |
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 | 0016310 | biological_process | phosphorylation |
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 | 0016310 | biological_process | phosphorylation |
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 | 0016310 | biological_process | phosphorylation |
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 | 0016310 | biological_process | phosphorylation |
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 | 6 |
Details | BINDING SITE FOR RESIDUE K A 533 |
Chain | Residue |
A | ASN74 |
A | SER76 |
A | ASP112 |
A | THR113 |
A | SER242 |
A | PEQ532 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MG A 534 |
Chain | Residue |
A | GLU271 |
A | ASP295 |
A | PEQ532 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE K B 533 |
Chain | Residue |
B | ASN74 |
B | SER76 |
B | ASP112 |
B | THR113 |
B | SER242 |
B | PEQ532 |
site_id | AC4 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE MG B 534 |
Chain | Residue |
B | GLU271 |
B | ASP295 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE K C 533 |
Chain | Residue |
C | ASN74 |
C | SER76 |
C | ASP112 |
C | THR113 |
C | PEQ532 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MG C 534 |
Chain | Residue |
C | GLU271 |
C | ASP295 |
C | HOH6071 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE K D 533 |
Chain | Residue |
D | ASN74 |
D | SER76 |
D | ASP112 |
D | THR113 |
D | PEQ532 |
site_id | AC8 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE MG D 534 |
Chain | Residue |
D | GLU271 |
D | ASP295 |
site_id | AC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE K E 533 |
Chain | Residue |
E | ASN74 |
E | SER76 |
E | ASP112 |
E | THR113 |
E | PEQ532 |
site_id | BC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG E 534 |
Chain | Residue |
E | LYS114 |
E | GLU271 |
E | ASP295 |
E | PEQ532 |
site_id | BC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE K F 533 |
Chain | Residue |
F | ASN74 |
F | SER76 |
F | ASP112 |
F | THR113 |
F | LYS114 |
F | SER242 |
F | PEQ532 |
site_id | BC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE MG F 534 |
Chain | Residue |
F | GLU271 |
F | ASP295 |
site_id | BC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE K G 533 |
Chain | Residue |
G | ASN74 |
G | SER76 |
G | ASP112 |
G | THR113 |
G | PEQ532 |
site_id | BC5 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE MG G 534 |
Chain | Residue |
G | GLU271 |
G | ASP295 |
site_id | BC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE K H 533 |
Chain | Residue |
H | ASN74 |
H | SER76 |
H | ASP112 |
H | THR113 |
H | LYS114 |
H | PEQ532 |
site_id | BC7 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE MG H 534 |
Chain | Residue |
H | GLU271 |
H | ASP295 |
site_id | BC8 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE PEQ A 532 |
Chain | Residue |
A | ARG72 |
A | LYS269 |
A | GLU271 |
A | ALA292 |
A | GLY294 |
A | ASP295 |
A | THR327 |
A | K533 |
A | MG534 |
site_id | BC9 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE PEQ B 532 |
Chain | Residue |
B | ARG72 |
B | LYS269 |
B | MET290 |
B | ALA292 |
B | GLY294 |
B | ASP295 |
B | THR327 |
B | K533 |
site_id | CC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PEQ C 532 |
Chain | Residue |
C | ARG72 |
C | LYS269 |
C | ASP295 |
C | THR327 |
C | K533 |
site_id | CC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE PEQ D 532 |
Chain | Residue |
D | ARG72 |
D | LYS269 |
D | GLU271 |
D | ALA292 |
D | GLY294 |
D | ASP295 |
D | THR327 |
D | K533 |
site_id | CC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE PEQ E 532 |
Chain | Residue |
E | ASP295 |
E | THR327 |
E | K533 |
E | MG534 |
E | ARG72 |
E | ASN74 |
E | LYS269 |
E | ALA292 |
site_id | CC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE PEQ F 532 |
Chain | Residue |
F | ARG72 |
F | LYS269 |
F | ALA292 |
F | GLY294 |
F | ASP295 |
F | THR327 |
F | K533 |
site_id | CC5 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE PEQ G 532 |
Chain | Residue |
G | ARG72 |
G | LYS269 |
G | GLU271 |
G | ALA292 |
G | GLY294 |
G | ASP295 |
G | THR327 |
G | K533 |
site_id | CC6 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE PEQ H 532 |
Chain | Residue |
H | ARG72 |
H | ASP112 |
H | LYS269 |
H | MET290 |
H | ALA292 |
H | GLY294 |
H | ASP295 |
H | THR327 |
H | K533 |
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 | VAL70 | |
A | GLU432 | |
H | PHE75 | |
H | HIS77 | |
H | PRO106 | |
H | THR113 | |
H | LYS114 | |
H | THR120 | |
H | GLY207 | |
H | ASN272 | |
H | GLU432 | |
H | LEU464 | |
A | LEU464 | |
H | ALA482 | |
H | VAL489 | |
H | PRO516 | |
A | ALA482 | |
A | VAL489 | |
A | PRO516 | |
B | VAL70 | |
B | PHE75 | |
B | HIS77 | |
B | PRO106 | |
B | THR113 | |
A | PHE75 | |
B | LYS114 | |
B | THR120 | |
B | GLY207 | |
B | ASN272 | |
B | GLU432 | |
B | LEU464 | |
B | ALA482 | |
B | VAL489 | |
B | PRO516 | |
C | VAL70 | |
A | HIS77 | |
C | PHE75 | |
C | HIS77 | |
C | PRO106 | |
C | THR113 | |
C | LYS114 | |
C | THR120 | |
C | GLY207 | |
C | ASN272 | |
C | GLU432 | |
C | LEU464 | |
A | PRO106 | |
C | ALA482 | |
C | VAL489 | |
C | PRO516 | |
D | VAL70 | |
D | PHE75 | |
D | HIS77 | |
D | PRO106 | |
D | THR113 | |
D | LYS114 | |
D | THR120 | |
A | THR113 | |
D | GLY207 | |
D | ASN272 | |
D | GLU432 | |
D | LEU464 | |
D | ALA482 | |
D | VAL489 | |
D | PRO516 | |
E | VAL70 | |
E | PHE75 | |
E | HIS77 | |
A | LYS114 | |
E | PRO106 | |
E | THR113 | |
E | LYS114 | |
E | THR120 | |
E | GLY207 | |
E | ASN272 | |
E | GLU432 | |
E | LEU464 | |
E | ALA482 | |
E | VAL489 | |
A | THR120 | |
E | PRO516 | |
F | VAL70 | |
F | PHE75 | |
F | HIS77 | |
F | PRO106 | |
F | THR113 | |
F | LYS114 | |
F | THR120 | |
F | GLY207 | |
F | ASN272 | |
A | GLY207 | |
F | GLU432 | |
F | LEU464 | |
F | ALA482 | |
F | VAL489 | |
F | PRO516 | |
G | VAL70 | |
G | PHE75 | |
G | HIS77 | |
G | PRO106 | |
G | THR113 | |
A | ASN272 | |
G | LYS114 | |
G | THR120 | |
G | GLY207 | |
G | ASN272 | |
G | GLU432 | |
G | LEU464 | |
G | ALA482 | |
G | VAL489 | |
G | PRO516 | |
H | VAL70 |
site_id | SWS_FT_FI2 |
Number of Residues | 40 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P30613 |
Chain | Residue | Details |
A | MET73 | |
B | GLN328 | |
C | MET73 | |
C | ILE270 | |
C | ASP295 | |
C | LEU296 | |
C | GLN328 | |
D | MET73 | |
D | ILE270 | |
D | ASP295 | |
D | LEU296 | |
A | ILE270 | |
D | GLN328 | |
E | MET73 | |
E | ILE270 | |
E | ASP295 | |
E | LEU296 | |
E | GLN328 | |
F | MET73 | |
F | ILE270 | |
F | ASP295 | |
F | LEU296 | |
A | ASP295 | |
F | GLN328 | |
G | MET73 | |
G | ILE270 | |
G | ASP295 | |
G | LEU296 | |
G | GLN328 | |
H | MET73 | |
H | ILE270 | |
H | ASP295 | |
H | LEU296 | |
A | LEU296 | |
H | GLN328 | |
A | GLN328 | |
B | MET73 | |
B | ILE270 | |
B | ASP295 | |
B | 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 | |
E | GLY127 | |
F | ALA37 | |
F | GLY127 | |
G | ALA37 | |
G | GLY127 | |
H | ALA37 | |
H | GLY127 | |
A | GLY127 | |
B | ALA37 | |
B | GLY127 | |
C | ALA37 | |
C | GLY127 | |
D | ALA37 | |
D | GLY127 | |
E | ALA37 |
site_id | SWS_FT_FI7 |
Number of Residues | 16 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P14618 |
Chain | Residue | Details |
A | ALA41 | |
E | GLU195 | |
F | ALA41 | |
F | GLU195 | |
G | ALA41 | |
G | GLU195 | |
H | ALA41 | |
H | GLU195 | |
A | GLU195 | |
B | ALA41 | |
B | GLU195 | |
C | ALA41 | |
C | GLU195 | |
D | ALA41 | |
D | GLU195 | |
E | ALA41 |
site_id | SWS_FT_FI8 |
Number of Residues | 24 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P14618 |
Chain | Residue | Details |
A | GLU62 | |
D | GLU62 | |
D | ASN89 | |
D | VAL305 | |
E | GLU62 | |
E | ASN89 | |
E | VAL305 | |
F | GLU62 | |
F | ASN89 | |
F | VAL305 | |
G | GLU62 | |
A | ASN89 | |
G | ASN89 | |
G | VAL305 | |
H | GLU62 | |
H | ASN89 | |
H | VAL305 | |
A | VAL305 | |
B | GLU62 | |
B | ASN89 | |
B | VAL305 | |
C | GLU62 | |
C | ASN89 | |
C | VAL305 |
site_id | SWS_FT_FI9 |
Number of Residues | 16 |
Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P52480 |
Chain | Residue | Details |
A | SER66 | |
E | ALA498 | |
F | SER66 | |
F | ALA498 | |
G | SER66 | |
G | ALA498 | |
H | SER66 | |
H | ALA498 | |
A | ALA498 | |
B | SER66 | |
B | ALA498 | |
C | SER66 | |
C | ALA498 | |
D | SER66 | |
D | ALA498 | |
E | SER66 |
site_id | SWS_FT_FI10 |
Number of Residues | 16 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P11980 |
Chain | Residue | Details |
A | PHE97 | |
E | ASP100 | |
F | PHE97 | |
F | ASP100 | |
G | PHE97 | |
G | ASP100 | |
H | PHE97 | |
H | ASP100 | |
A | ASP100 | |
B | PHE97 | |
B | ASP100 | |
C | PHE97 | |
C | ASP100 | |
D | PHE97 | |
D | ASP100 | |
E | PHE97 |
site_id | SWS_FT_FI11 |
Number of Residues | 16 |
Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P14618 |
Chain | Residue | Details |
A | ARG105 | |
E | VAL175 | |
F | ARG105 | |
F | VAL175 | |
G | ARG105 | |
G | VAL175 | |
H | ARG105 | |
H | VAL175 | |
A | VAL175 | |
B | ARG105 | |
B | VAL175 | |
C | ARG105 | |
C | VAL175 | |
D | ARG105 | |
D | VAL175 | |
E | ARG105 |
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 | |
E | PRO322 | |
F | VAL166 | |
F | PRO322 | |
G | VAL166 | |
G | PRO322 | |
H | VAL166 | |
H | PRO322 | |
A | PRO322 | |
B | VAL166 | |
B | PRO322 | |
C | VAL166 | |
C | PRO322 | |
D | VAL166 | |
D | PRO322 | |
E | VAL166 |
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 |
D | ILE266 | |
D | ILE270 | |
E | ILE266 | |
E | ILE270 | |
F | ILE266 | |
F | ILE270 | |
A | ILE266 | |
G | ILE266 | |
G | ILE270 | |
H | ILE266 | |
H | ILE270 | |
A | ILE270 | |
B | ILE266 | |
B | ILE270 | |
C | ILE266 | |
C | 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 | CSA1 |
Number of Residues | 6 |
Details | Annotated By Reference To The Literature 1pkn |
Chain | Residue | Details |
A | LYS269 | |
A | SER361 | |
A | ARG119 | |
A | GLU363 | |
A | ARG72 | |
A | THR327 |
site_id | CSA2 |
Number of Residues | 6 |
Details | Annotated By Reference To The Literature 1pkn |
Chain | Residue | Details |
B | LYS269 | |
B | SER361 | |
B | ARG119 | |
B | GLU363 | |
B | ARG72 | |
B | THR327 |
site_id | CSA3 |
Number of Residues | 6 |
Details | Annotated By Reference To The Literature 1pkn |
Chain | Residue | Details |
C | LYS269 | |
C | SER361 | |
C | ARG119 | |
C | GLU363 | |
C | ARG72 | |
C | THR327 |
site_id | CSA4 |
Number of Residues | 6 |
Details | Annotated By Reference To The Literature 1pkn |
Chain | Residue | Details |
D | LYS269 | |
D | SER361 | |
D | ARG119 | |
D | GLU363 | |
D | ARG72 | |
D | THR327 |
site_id | CSA5 |
Number of Residues | 5 |
Details | Annotated By Reference To The Literature 1pkn |
Chain | Residue | Details |
E | SER361 | |
E | LYS269 | |
E | GLU363 | |
E | ARG72 | |
E | THR327 |
site_id | CSA6 |
Number of Residues | 6 |
Details | Annotated By Reference To The Literature 1pkn |
Chain | Residue | Details |
F | LYS269 | |
F | SER361 | |
F | ARG119 | |
F | GLU363 | |
F | ARG72 | |
F | THR327 |
site_id | CSA7 |
Number of Residues | 6 |
Details | Annotated By Reference To The Literature 1pkn |
Chain | Residue | Details |
G | LYS269 | |
G | SER361 | |
G | ARG119 | |
G | GLU363 | |
G | ARG72 | |
G | THR327 |
site_id | CSA8 |
Number of Residues | 6 |
Details | Annotated By Reference To The Literature 1pkn |
Chain | Residue | Details |
H | LYS269 | |
H | SER361 | |
H | ARG119 | |
H | GLU363 | |
H | ARG72 | |
H | THR327 |
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 |