1A49
BIS MG-ATP-K-OXALATE COMPLEX OF PYRUVATE KINASE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| 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 | 0016740 | molecular_function | transferase activity |
| A | 0030955 | molecular_function | potassium ion binding |
| 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 | 0000166 | molecular_function | nucleotide binding |
| 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 | 0016740 | molecular_function | transferase activity |
| B | 0030955 | molecular_function | potassium ion binding |
| 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 | 0000166 | molecular_function | nucleotide binding |
| 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 | 0016740 | molecular_function | transferase activity |
| C | 0030955 | molecular_function | potassium ion binding |
| 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 | 0000166 | molecular_function | nucleotide binding |
| 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 | 0016740 | molecular_function | transferase activity |
| D | 0030955 | molecular_function | potassium ion binding |
| 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 | 0000166 | molecular_function | nucleotide binding |
| 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 | 0016740 | molecular_function | transferase activity |
| E | 0030955 | molecular_function | potassium ion binding |
| 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 | 0000166 | molecular_function | nucleotide binding |
| 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 | 0016740 | molecular_function | transferase activity |
| F | 0030955 | molecular_function | potassium ion binding |
| 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 | 0000166 | molecular_function | nucleotide binding |
| 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 | 0016740 | molecular_function | transferase activity |
| G | 0030955 | molecular_function | potassium ion binding |
| 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 | 0000166 | molecular_function | nucleotide binding |
| 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 | 0016740 | molecular_function | transferase activity |
| H | 0030955 | molecular_function | potassium ion binding |
| 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 532 |
| Chain | Residue |
| A | ASN74 |
| A | SER76 |
| A | ASP112 |
| A | THR113 |
| A | SER242 |
| A | ATP535 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE OXL A 533 |
| Chain | Residue |
| A | MET290 |
| A | ALA292 |
| A | ARG293 |
| A | GLY294 |
| A | ASP295 |
| A | THR327 |
| A | MG534 |
| A | ATP535 |
| A | HOH6763 |
| A | ARG72 |
| A | LYS269 |
| A | GLU271 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 534 |
| Chain | Residue |
| A | GLU271 |
| A | ASP295 |
| A | OXL533 |
| A | ATP535 |
| A | HOH6763 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG A 536 |
| Chain | Residue |
| A | ATP535 |
| A | HOH6079 |
| A | HOH6469 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K B 1132 |
| Chain | Residue |
| B | ASN674 |
| B | SER676 |
| B | ASP712 |
| B | THR713 |
| B | HOH6141 |
| site_id | AC6 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE OXL B 1133 |
| Chain | Residue |
| B | LYS869 |
| B | GLU871 |
| B | MET890 |
| B | ALA892 |
| B | ARG893 |
| B | GLY894 |
| B | ASP895 |
| B | THR927 |
| B | MG1134 |
| B | HOH6624 |
| B | HOH7031 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG B 1134 |
| Chain | Residue |
| B | GLU871 |
| B | ASP895 |
| B | OXL1133 |
| B | HOH7031 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE K C 1732 |
| Chain | Residue |
| C | ASN1274 |
| C | SER1276 |
| C | ASP1312 |
| C | THR1313 |
| C | SER1442 |
| C | ATP1735 |
| C | HOH7921 |
| site_id | AC9 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE OXL C 1733 |
| Chain | Residue |
| C | ARG1272 |
| C | LYS1469 |
| C | GLU1471 |
| C | ALA1492 |
| C | ARG1493 |
| C | GLY1494 |
| C | ASP1495 |
| C | THR1527 |
| C | MG1734 |
| C | ATP1735 |
| C | HOH6663 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG C 1734 |
| Chain | Residue |
| C | LYS1469 |
| C | GLU1471 |
| C | ASP1495 |
| C | OXL1733 |
| C | ATP1735 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG C 1736 |
| Chain | Residue |
| C | ATP1735 |
| C | HOH6006 |
| C | HOH6581 |
| C | HOH6663 |
| site_id | BC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE K D 2332 |
| Chain | Residue |
| D | ASN1874 |
| D | SER1876 |
| D | ASP1912 |
| D | THR1913 |
| D | SER2042 |
| D | ATP2335 |
| D | HOH7499 |
| site_id | BC4 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE OXL D 2333 |
| Chain | Residue |
| D | LYS2069 |
| D | GLU2071 |
| D | MET2090 |
| D | ALA2092 |
| D | ARG2093 |
| D | GLY2094 |
| D | ASP2095 |
| D | THR2127 |
| D | MET2159 |
| D | MG2334 |
| D | ATP2335 |
| D | HOH6045 |
| D | HOH6387 |
| site_id | BC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG D 2334 |
| Chain | Residue |
| D | GLU2071 |
| D | ASP2095 |
| D | OXL2333 |
| D | ATP2335 |
| D | HOH6439 |
| site_id | BC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG D 2336 |
| Chain | Residue |
| D | HOH6045 |
| D | HOH6387 |
| D | HOH7364 |
| D | ATP2335 |
| site_id | BC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE K E 3532 |
| Chain | Residue |
| E | ASN3074 |
| E | SER3076 |
| E | ASP3112 |
| E | THR3113 |
| E | SER3242 |
| E | ATP3535 |
| E | HOH7785 |
| site_id | BC8 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE OXL E 3533 |
| Chain | Residue |
| E | LYS3269 |
| E | GLU3271 |
| E | ALA3292 |
| E | ARG3293 |
| E | GLY3294 |
| E | ASP3295 |
| E | THR3327 |
| E | MG3534 |
| E | ATP3535 |
| E | HOH6162 |
| E | HOH6348 |
| E | HOH6988 |
| site_id | BC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG E 3534 |
| Chain | Residue |
| E | GLU3271 |
| E | ASP3295 |
| E | OXL3533 |
| E | ATP3535 |
| E | HOH6988 |
| site_id | CC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG E 3536 |
| Chain | Residue |
| E | ATP3535 |
| E | HOH6162 |
| E | HOH6348 |
| E | HOH7443 |
| site_id | CC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE K F 4132 |
| Chain | Residue |
| F | ASN3674 |
| F | SER3676 |
| F | ASP3712 |
| F | THR3713 |
| F | SER3842 |
| F | ATP4135 |
| F | HOH6491 |
| site_id | CC3 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE OXL F 4133 |
| Chain | Residue |
| F | ARG3672 |
| F | LYS3869 |
| F | GLU3871 |
| F | MET3890 |
| F | ALA3892 |
| F | ARG3893 |
| F | GLY3894 |
| F | ASP3895 |
| F | THR3927 |
| F | MG4134 |
| F | ATP4135 |
| F | HOH6300 |
| F | HOH6460 |
| site_id | CC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG F 4134 |
| Chain | Residue |
| F | GLU3871 |
| F | ASP3895 |
| F | OXL4133 |
| F | ATP4135 |
| F | HOH6460 |
| site_id | CC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG F 4136 |
| Chain | Residue |
| F | ATP4135 |
| F | HOH6300 |
| F | HOH7054 |
| F | HOH7055 |
| site_id | CC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE K G 4732 |
| Chain | Residue |
| G | ASN4274 |
| G | SER4276 |
| G | ASP4312 |
| G | THR4313 |
| G | SER4442 |
| G | ATP4735 |
| G | HOH7049 |
| site_id | CC7 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE OXL G 4733 |
| Chain | Residue |
| G | ARG4272 |
| G | LYS4469 |
| G | GLU4471 |
| G | ALA4492 |
| G | ARG4493 |
| G | GLY4494 |
| G | ASP4495 |
| G | THR4527 |
| G | MG4734 |
| G | ATP4735 |
| G | HOH6349 |
| G | HOH6671 |
| site_id | CC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG G 4734 |
| Chain | Residue |
| G | GLU4471 |
| G | ASP4495 |
| G | OXL4733 |
| G | ATP4735 |
| G | HOH6671 |
| site_id | CC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG G 4736 |
| Chain | Residue |
| G | ATP4735 |
| G | HOH6177 |
| G | HOH6256 |
| G | HOH6349 |
| site_id | DC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K H 5332 |
| Chain | Residue |
| H | ASN4874 |
| H | SER4876 |
| H | ASP4912 |
| H | THR4913 |
| H | HOH6838 |
| H | HOH6965 |
| site_id | DC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE OXL H 5333 |
| Chain | Residue |
| H | LYS5069 |
| H | GLU5071 |
| H | MET5090 |
| H | ALA5092 |
| H | ARG5093 |
| H | GLY5094 |
| H | ASP5095 |
| H | THR5127 |
| H | MG5334 |
| H | HOH7293 |
| site_id | DC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG H 5334 |
| Chain | Residue |
| H | LYS5069 |
| H | GLU5071 |
| H | ASP5095 |
| H | OXL5333 |
| H | HOH7292 |
| H | HOH7293 |
| site_id | DC4 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE ATP A 535 |
| Chain | Residue |
| A | PRO52 |
| A | ARG72 |
| A | ASN74 |
| A | HIS77 |
| A | TYR82 |
| A | HIS83 |
| A | ARG119 |
| A | LYS206 |
| A | ASP295 |
| A | SER361 |
| A | LYS366 |
| A | K532 |
| A | OXL533 |
| A | MG534 |
| A | MG536 |
| A | HOH6003 |
| A | HOH6079 |
| A | HOH6366 |
| A | HOH6469 |
| A | HOH6995 |
| A | HOH7738 |
| A | HOH7743 |
| site_id | DC5 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE ATP C 1735 |
| Chain | Residue |
| C | THR1249 |
| C | PRO1252 |
| C | ARG1272 |
| C | ASN1274 |
| C | HIS1277 |
| C | TYR1282 |
| C | HIS1283 |
| C | ARG1319 |
| C | LYS1406 |
| C | ASP1495 |
| C | SER1561 |
| C | LYS1566 |
| C | K1732 |
| C | OXL1733 |
| C | MG1734 |
| C | MG1736 |
| C | HOH6005 |
| C | HOH6006 |
| C | HOH6581 |
| C | HOH6663 |
| C | HOH6879 |
| C | HOH7844 |
| site_id | DC6 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE ATP D 2335 |
| Chain | Residue |
| D | THR1849 |
| D | PRO1852 |
| D | ARG1872 |
| D | ASN1874 |
| D | HIS1877 |
| D | TYR1882 |
| D | ARG1919 |
| D | LYS2006 |
| D | ASP2095 |
| D | SER2161 |
| D | LYS2166 |
| D | K2332 |
| D | OXL2333 |
| D | MG2334 |
| D | MG2336 |
| D | HOH6004 |
| D | HOH6045 |
| D | HOH6082 |
| D | HOH6140 |
| D | HOH6387 |
| D | HOH6463 |
| D | HOH6745 |
| D | HOH7364 |
| D | HOH7874 |
| site_id | DC7 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE ATP E 3535 |
| Chain | Residue |
| E | THR3049 |
| E | PRO3052 |
| E | ARG3072 |
| E | ASN3074 |
| E | HIS3077 |
| E | TYR3082 |
| E | HIS3083 |
| E | ARG3119 |
| E | LYS3206 |
| E | ASP3295 |
| E | SER3361 |
| E | ALA3365 |
| E | LYS3366 |
| E | K3532 |
| E | OXL3533 |
| E | MG3534 |
| E | MG3536 |
| E | HOH6159 |
| E | HOH6162 |
| E | HOH6222 |
| E | HOH6318 |
| E | HOH6348 |
| E | HOH6498 |
| E | HOH7137 |
| E | HOH7443 |
| E | HOH7793 |
| site_id | DC8 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE ATP F 4135 |
| Chain | Residue |
| F | PRO3652 |
| F | ARG3672 |
| F | ASN3674 |
| F | HIS3677 |
| F | TYR3682 |
| F | ARG3719 |
| F | LYS3869 |
| F | ASP3895 |
| F | SER3961 |
| F | LYS3966 |
| F | K4132 |
| F | OXL4133 |
| F | MG4134 |
| F | MG4136 |
| F | HOH6178 |
| F | HOH6300 |
| F | HOH6460 |
| F | HOH7054 |
| F | HOH7055 |
| F | HOH7453 |
| F | HOH7923 |
| site_id | DC9 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE ATP G 4735 |
| Chain | Residue |
| G | THR4249 |
| G | PRO4252 |
| G | ARG4272 |
| G | ASN4274 |
| G | HIS4277 |
| G | TYR4282 |
| G | HIS4283 |
| G | ARG4319 |
| G | LYS4406 |
| G | ASP4495 |
| G | SER4561 |
| G | GLY4562 |
| G | ALA4565 |
| G | K4732 |
| G | OXL4733 |
| G | MG4734 |
| G | MG4736 |
| G | HOH6177 |
| G | HOH6179 |
| G | HOH6256 |
| G | HOH6349 |
| G | HOH6534 |
| G | HOH6637 |
| G | HOH6671 |
| G | HOH7330 |
| G | HOH7663 |
| G | HOH7924 |
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 | 1792 |
| Details | Region: {"description":"Interaction with POU5F1","evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 200 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 40 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P30613","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | Site: {"description":"Transition state stabilizer","evidences":[{"source":"UniProtKB","id":"P00549","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 16 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 16 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 24 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 16 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P52480","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 16 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P11980","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 16 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 8 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P52480","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 16 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P52480","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 8 |
| Details | Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 8 |
| Details | Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P52480","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| Number of Residues | 8 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P52480","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI16 |
| Number of Residues | 8 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI17 |
| Number of Residues | 24 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI18 |
| Number of Residues | 8 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate","evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI19 |
| Number of Residues | 16 |
| Details | Modified residue: {"description":"S-nitrosocysteine","evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
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 | LYS869 | |
| B | ARG719 | |
| B | ARG672 | |
| B | THR927 | |
| B | SER961 | |
| B | GLU963 |
| site_id | CSA3 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1pkn |
| Chain | Residue | Details |
| C | ARG1319 | |
| C | SER1561 | |
| C | LYS1469 | |
| C | GLU1563 | |
| C | THR1527 | |
| C | ARG1272 |
| site_id | CSA4 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1pkn |
| Chain | Residue | Details |
| D | SER2161 | |
| D | ARG1919 | |
| D | GLU2163 | |
| D | THR2127 | |
| D | ARG1872 | |
| D | LYS2069 |
| site_id | CSA5 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1pkn |
| Chain | Residue | Details |
| E | GLU3363 | |
| E | THR3327 | |
| E | ARG3072 | |
| E | SER3361 | |
| E | ARG3119 | |
| E | LYS3269 |
| site_id | CSA6 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1pkn |
| Chain | Residue | Details |
| F | LYS3869 | |
| F | THR3927 | |
| F | SER3961 | |
| F | ARG3672 | |
| F | GLU3963 | |
| F | ARG3719 |
| site_id | CSA7 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1pkn |
| Chain | Residue | Details |
| G | ARG4319 | |
| G | SER4561 | |
| G | GLU4563 | |
| G | LYS4469 | |
| G | ARG4272 | |
| G | THR4527 |
| site_id | CSA8 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1pkn |
| Chain | Residue | Details |
| H | SER5161 | |
| H | ARG4919 | |
| H | GLU5163 | |
| H | THR5127 | |
| H | LYS5069 | |
| H | ARG4872 |
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 326 |
| Chain | Residue | Details |
| A | ARG72 | attractive charge-charge interaction, electrostatic stabiliser, steric role |
| A | ARG119 | attractive charge-charge interaction, electrostatic stabiliser, steric role |
| A | LYS269 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, steric role |
| A | THR327 | electrostatic stabiliser, hydrogen bond donor, increase acidity |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 326 |
| Chain | Residue | Details |
| B | ARG672 | attractive charge-charge interaction, electrostatic stabiliser, steric role |
| B | ARG719 | attractive charge-charge interaction, electrostatic stabiliser, steric role |
| B | LYS869 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, steric role |
| B | THR927 | electrostatic stabiliser, hydrogen bond donor, increase acidity |
| site_id | MCSA3 |
| Number of Residues | 4 |
| Details | M-CSA 326 |
| Chain | Residue | Details |
| C | ARG1272 | attractive charge-charge interaction, electrostatic stabiliser, steric role |
| C | ARG1319 | attractive charge-charge interaction, electrostatic stabiliser, steric role |
| C | LYS1469 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, steric role |
| C | THR1527 | electrostatic stabiliser, hydrogen bond donor, increase acidity |
| site_id | MCSA4 |
| Number of Residues | 4 |
| Details | M-CSA 326 |
| Chain | Residue | Details |
| D | ARG1872 | attractive charge-charge interaction, electrostatic stabiliser, steric role |
| D | ARG1919 | attractive charge-charge interaction, electrostatic stabiliser, steric role |
| D | LYS2069 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, steric role |
| D | THR2127 | electrostatic stabiliser, hydrogen bond donor, increase acidity |
| site_id | MCSA5 |
| Number of Residues | 4 |
| Details | M-CSA 326 |
| Chain | Residue | Details |
| E | ARG3072 | attractive charge-charge interaction, electrostatic stabiliser, steric role |
| E | ARG3119 | attractive charge-charge interaction, electrostatic stabiliser, steric role |
| E | LYS3269 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, steric role |
| E | THR3327 | electrostatic stabiliser, hydrogen bond donor, increase acidity |
| site_id | MCSA6 |
| Number of Residues | 4 |
| Details | M-CSA 326 |
| Chain | Residue | Details |
| F | ARG3672 | attractive charge-charge interaction, electrostatic stabiliser, steric role |
| F | ARG3719 | attractive charge-charge interaction, electrostatic stabiliser, steric role |
| F | LYS3869 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, steric role |
| F | THR3927 | electrostatic stabiliser, hydrogen bond donor, increase acidity |
| site_id | MCSA7 |
| Number of Residues | 4 |
| Details | M-CSA 326 |
| Chain | Residue | Details |
| G | ARG4272 | attractive charge-charge interaction, electrostatic stabiliser, steric role |
| G | ARG4319 | attractive charge-charge interaction, electrostatic stabiliser, steric role |
| G | LYS4469 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, steric role |
| G | THR4527 | electrostatic stabiliser, hydrogen bond donor, increase acidity |
| site_id | MCSA8 |
| Number of Residues | 4 |
| Details | M-CSA 326 |
| Chain | Residue | Details |
| H | ARG4872 | attractive charge-charge interaction, electrostatic stabiliser, steric role |
| H | ARG4919 | attractive charge-charge interaction, electrostatic stabiliser, steric role |
| H | LYS5069 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, steric role |
| H | THR5127 | electrostatic stabiliser, hydrogen bond donor, increase acidity |
