1F3X
S402P MUTANT OF RABBIT 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 | 4 |
| Details | BINDING SITE FOR RESIDUE K A 531 |
| Chain | Residue |
| A | ASN74 |
| A | SER76 |
| A | ASP112 |
| A | THR113 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K B 532 |
| Chain | Residue |
| B | HOH1034 |
| B | ASN74 |
| B | SER76 |
| B | ASP112 |
| B | THR113 |
| B | SER242 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K C 533 |
| Chain | Residue |
| C | ASN74 |
| C | SER76 |
| C | ASP112 |
| C | THR113 |
| C | SER242 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE K D 534 |
| Chain | Residue |
| D | ASN74 |
| D | SER76 |
| D | ASP112 |
| D | THR113 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE K E 535 |
| Chain | Residue |
| E | ASN74 |
| E | SER76 |
| E | ASP112 |
| E | THR113 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K F 536 |
| Chain | Residue |
| F | ASN74 |
| F | SER76 |
| F | ASP112 |
| F | THR113 |
| F | SER242 |
| F | HOH2034 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K G 537 |
| Chain | Residue |
| G | ASN74 |
| G | SER76 |
| G | ASP112 |
| G | THR113 |
| G | SER242 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE K H 538 |
| Chain | Residue |
| H | ASN74 |
| H | SER76 |
| H | ASP112 |
| H | THR113 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MN A 532 |
| Chain | Residue |
| A | GLU271 |
| A | ASP295 |
| A | PYR541 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN B 533 |
| Chain | Residue |
| B | LYS269 |
| B | GLU271 |
| B | ASP295 |
| B | PYR542 |
| B | HOH941 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MN C 532 |
| Chain | Residue |
| C | GLU271 |
| C | ASP295 |
| C | PYR543 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MN D 532 |
| Chain | Residue |
| D | LYS269 |
| D | GLU271 |
| D | ASP295 |
| D | PYR544 |
| site_id | BC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MN E 532 |
| Chain | Residue |
| E | GLU271 |
| E | ASP295 |
| E | PYR545 |
| site_id | BC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN F 532 |
| Chain | Residue |
| F | LYS269 |
| F | GLU271 |
| F | ASP295 |
| F | PYR546 |
| F | HOH1941 |
| site_id | BC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MN G 532 |
| Chain | Residue |
| G | GLU271 |
| G | ASP295 |
| G | PYR547 |
| site_id | BC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MN H 532 |
| Chain | Residue |
| H | LYS269 |
| H | GLU271 |
| H | ASP295 |
| H | PYR548 |
| site_id | BC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PYR A 541 |
| Chain | Residue |
| A | ARG72 |
| A | LYS269 |
| A | GLU271 |
| A | ALA292 |
| A | ARG293 |
| A | GLY294 |
| A | ASP295 |
| A | THR327 |
| A | MN532 |
| site_id | BC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PYR B 542 |
| Chain | Residue |
| B | LYS269 |
| B | GLU271 |
| B | ALA292 |
| B | GLY294 |
| B | ASP295 |
| B | THR327 |
| B | MN533 |
| B | HOH941 |
| site_id | CC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PYR C 543 |
| Chain | Residue |
| C | LYS269 |
| C | GLU271 |
| C | ALA292 |
| C | GLY294 |
| C | ASP295 |
| C | THR327 |
| C | MN532 |
| C | HOH978 |
| site_id | CC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PYR D 544 |
| Chain | Residue |
| D | ASP295 |
| D | THR327 |
| D | MN532 |
| D | ARG72 |
| D | LYS269 |
| D | GLU271 |
| D | ALA292 |
| D | ARG293 |
| D | GLY294 |
| site_id | CC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PYR E 545 |
| Chain | Residue |
| E | ARG72 |
| E | LYS269 |
| E | GLU271 |
| E | MET290 |
| E | ALA292 |
| E | ARG293 |
| E | GLY294 |
| E | ASP295 |
| E | THR327 |
| E | MN532 |
| site_id | CC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PYR F 546 |
| Chain | Residue |
| F | LYS269 |
| F | GLU271 |
| F | ALA292 |
| F | GLY294 |
| F | ASP295 |
| F | THR327 |
| F | MN532 |
| F | HOH1941 |
| site_id | CC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PYR G 547 |
| Chain | Residue |
| G | ARG72 |
| G | LYS269 |
| G | GLU271 |
| G | ALA292 |
| G | GLY294 |
| G | ASP295 |
| G | THR327 |
| G | MN532 |
| G | HOH1978 |
| site_id | CC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PYR H 548 |
| Chain | Residue |
| H | ARG72 |
| H | LYS269 |
| H | GLU271 |
| H | ALA292 |
| H | ARG293 |
| H | GLY294 |
| H | ASP295 |
| H | THR327 |
| H | MN532 |
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 | 6 |
| Details | Annotated By Reference To The Literature 1pkn |
| Chain | Residue | Details |
| E | LYS269 | |
| E | SER361 | |
| E | ARG119 | |
| 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 |
