3G2G
S437Y Mutant of human muscle pyruvate kinase, isoform M2
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0003723 | molecular_function | RNA 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 | 0005576 | cellular_component | extracellular region |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005791 | cellular_component | rough endoplasmic reticulum |
| A | 0005829 | cellular_component | cytosol |
| A | 0005929 | cellular_component | cilium |
| A | 0006096 | biological_process | glycolytic process |
| A | 0006417 | biological_process | regulation of translation |
| A | 0012501 | biological_process | programmed cell death |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016310 | biological_process | phosphorylation |
| A | 0023026 | molecular_function | MHC class II protein complex binding |
| A | 0030955 | molecular_function | potassium ion binding |
| A | 0031982 | cellular_component | vesicle |
| A | 0032869 | biological_process | cellular response to insulin stimulus |
| A | 0034774 | cellular_component | secretory granule lumen |
| A | 0045296 | molecular_function | cadherin binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0061621 | biological_process | canonical glycolysis |
| A | 0062023 | cellular_component | collagen-containing extracellular matrix |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 1903561 | cellular_component | extracellular vesicle |
| A | 1903672 | biological_process | positive regulation of sprouting angiogenesis |
| A | 1904813 | cellular_component | ficolin-1-rich granule lumen |
| A | 2000767 | biological_process | positive regulation of cytoplasmic translation |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0003723 | molecular_function | RNA 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 | 0005576 | cellular_component | extracellular region |
| B | 0005634 | cellular_component | nucleus |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005791 | cellular_component | rough endoplasmic reticulum |
| B | 0005829 | cellular_component | cytosol |
| B | 0005929 | cellular_component | cilium |
| B | 0006096 | biological_process | glycolytic process |
| B | 0006417 | biological_process | regulation of translation |
| B | 0012501 | biological_process | programmed cell death |
| B | 0016301 | molecular_function | kinase activity |
| B | 0016310 | biological_process | phosphorylation |
| B | 0023026 | molecular_function | MHC class II protein complex binding |
| B | 0030955 | molecular_function | potassium ion binding |
| B | 0031982 | cellular_component | vesicle |
| B | 0032869 | biological_process | cellular response to insulin stimulus |
| B | 0034774 | cellular_component | secretory granule lumen |
| B | 0045296 | molecular_function | cadherin binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0061621 | biological_process | canonical glycolysis |
| B | 0062023 | cellular_component | collagen-containing extracellular matrix |
| B | 0070062 | cellular_component | extracellular exosome |
| B | 1903561 | cellular_component | extracellular vesicle |
| B | 1903672 | biological_process | positive regulation of sprouting angiogenesis |
| B | 1904813 | cellular_component | ficolin-1-rich granule lumen |
| B | 2000767 | biological_process | positive regulation of cytoplasmic translation |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0003723 | molecular_function | RNA 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 | 0005576 | cellular_component | extracellular region |
| C | 0005634 | cellular_component | nucleus |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005739 | cellular_component | mitochondrion |
| C | 0005791 | cellular_component | rough endoplasmic reticulum |
| C | 0005829 | cellular_component | cytosol |
| C | 0005929 | cellular_component | cilium |
| C | 0006096 | biological_process | glycolytic process |
| C | 0006417 | biological_process | regulation of translation |
| C | 0012501 | biological_process | programmed cell death |
| C | 0016301 | molecular_function | kinase activity |
| C | 0016310 | biological_process | phosphorylation |
| C | 0023026 | molecular_function | MHC class II protein complex binding |
| C | 0030955 | molecular_function | potassium ion binding |
| C | 0031982 | cellular_component | vesicle |
| C | 0032869 | biological_process | cellular response to insulin stimulus |
| C | 0034774 | cellular_component | secretory granule lumen |
| C | 0045296 | molecular_function | cadherin binding |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0061621 | biological_process | canonical glycolysis |
| C | 0062023 | cellular_component | collagen-containing extracellular matrix |
| C | 0070062 | cellular_component | extracellular exosome |
| C | 1903561 | cellular_component | extracellular vesicle |
| C | 1903672 | biological_process | positive regulation of sprouting angiogenesis |
| C | 1904813 | cellular_component | ficolin-1-rich granule lumen |
| C | 2000767 | biological_process | positive regulation of cytoplasmic translation |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0003723 | molecular_function | RNA 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 | 0005576 | cellular_component | extracellular region |
| D | 0005634 | cellular_component | nucleus |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005739 | cellular_component | mitochondrion |
| D | 0005791 | cellular_component | rough endoplasmic reticulum |
| D | 0005829 | cellular_component | cytosol |
| D | 0005929 | cellular_component | cilium |
| D | 0006096 | biological_process | glycolytic process |
| D | 0006417 | biological_process | regulation of translation |
| D | 0012501 | biological_process | programmed cell death |
| D | 0016301 | molecular_function | kinase activity |
| D | 0016310 | biological_process | phosphorylation |
| D | 0023026 | molecular_function | MHC class II protein complex binding |
| D | 0030955 | molecular_function | potassium ion binding |
| D | 0031982 | cellular_component | vesicle |
| D | 0032869 | biological_process | cellular response to insulin stimulus |
| D | 0034774 | cellular_component | secretory granule lumen |
| D | 0045296 | molecular_function | cadherin binding |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0061621 | biological_process | canonical glycolysis |
| D | 0062023 | cellular_component | collagen-containing extracellular matrix |
| D | 0070062 | cellular_component | extracellular exosome |
| D | 1903561 | cellular_component | extracellular vesicle |
| D | 1903672 | biological_process | positive regulation of sprouting angiogenesis |
| D | 1904813 | cellular_component | ficolin-1-rich granule lumen |
| D | 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 SO4 A 532 |
| Chain | Residue |
| A | THR432 |
| A | LYS433 |
| A | SER434 |
| A | ARG436 |
| A | TYR437 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 533 |
| Chain | Residue |
| A | HIS274 |
| A | GLU275 |
| A | ARG278 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE UNX A 535 |
| Chain | Residue |
| A | LYS433 |
| A | ARG455 |
| A | THR432 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE UNX A 536 |
| Chain | Residue |
| A | ARG342 |
| A | SER346 |
| B | VAL306 |
| B | HOH566 |
| B | HOH600 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE UNX A 537 |
| Chain | Residue |
| A | ASN75 |
| A | SER77 |
| A | ASP113 |
| A | THR114 |
| A | HOH588 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 532 |
| Chain | Residue |
| B | THR432 |
| B | LYS433 |
| B | SER434 |
| B | ARG436 |
| B | TYR437 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 533 |
| Chain | Residue |
| B | SER77 |
| B | HIS78 |
| B | GLY79 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 534 |
| Chain | Residue |
| B | HIS274 |
| B | GLU275 |
| B | ARG278 |
| B | HOH619 |
| D | HOH580 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE UNX B 535 |
| Chain | Residue |
| B | ASN75 |
| B | SER77 |
| B | ASP113 |
| B | THR114 |
| B | LYS270 |
| B | HOH652 |
| site_id | BC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE UNX B 536 |
| Chain | Residue |
| B | ARG73 |
| site_id | BC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE UNX B 537 |
| Chain | Residue |
| B | HIS78 |
| B | ARG120 |
| site_id | BC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE UNX B 538 |
| Chain | Residue |
| B | GLU260 |
| B | LYS261 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE UNX B 539 |
| Chain | Residue |
| B | ALA293 |
| B | ARG294 |
| B | GLY295 |
| B | THR328 |
| site_id | BC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE UNX B 540 |
| Chain | Residue |
| B | GLY46 |
| B | ASN70 |
| B | HIS464 |
| B | HOH549 |
| site_id | BC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE UNX B 541 |
| Chain | Residue |
| B | CYS317 |
| B | ASN318 |
| B | LYS322 |
| B | ASP357 |
| B | ARG445 |
| B | HOH560 |
| site_id | BC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE UNX B 542 |
| Chain | Residue |
| A | THR341 |
| A | ALA343 |
| B | GLN329 |
| B | GLU332 |
| B | GLU344 |
| site_id | BC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE UNX B 543 |
| Chain | Residue |
| A | ASN350 |
| B | GLN310 |
| B | LYS311 |
| B | ASN350 |
| B | ASP354 |
| B | HOH561 |
| site_id | BC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE UNX B 544 |
| Chain | Residue |
| B | MET334 |
| B | ILE335 |
| B | GLU364 |
| B | GLY368 |
| B | ASP369 |
| B | TYR370 |
| B | PRO371 |
| site_id | CC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE UNX B 545 |
| Chain | Residue |
| B | VAL251 |
| B | HIS252 |
| B | ARG255 |
| B | ALA286 |
| site_id | CC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE UNX B 546 |
| Chain | Residue |
| B | ARG279 |
| B | ASP281 |
| B | GLU282 |
| B | HOH563 |
| B | HOH672 |
| site_id | CC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 C 532 |
| Chain | Residue |
| C | THR432 |
| C | LYS433 |
| C | SER434 |
| C | ARG436 |
| C | TYR437 |
| site_id | CC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 C 533 |
| Chain | Residue |
| C | HIS78 |
| C | GLY79 |
| C | LYS206 |
| site_id | CC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 C 534 |
| Chain | Residue |
| C | HIS78 |
| C | ARG120 |
| C | HOH603 |
| C | HOH633 |
| C | HOH652 |
| site_id | CC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 C 535 |
| Chain | Residue |
| C | HIS274 |
| C | GLU275 |
| C | ARG278 |
| site_id | CC7 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE UNX C 536 |
| Chain | Residue |
| C | ARG73 |
| site_id | CC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE UNX C 537 |
| Chain | Residue |
| C | THR432 |
| C | ARG455 |
| C | HOH579 |
| site_id | CC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE UNX C 538 |
| Chain | Residue |
| C | LEU380 |
| C | ARG383 |
| C | GLU384 |
| C | HOH595 |
| site_id | DC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE UNX C 539 |
| Chain | Residue |
| C | ASN75 |
| C | SER77 |
| C | ASP113 |
| C | THR114 |
| C | HOH566 |
| site_id | DC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE UNX C 540 |
| Chain | Residue |
| C | THR95 |
| C | TYR105 |
| C | PRO107 |
| C | VAL108 |
| C | ARG461 |
| C | HOH625 |
| site_id | DC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE UNX C 541 |
| Chain | Residue |
| C | GLN17 |
| C | ALA20 |
| C | ARG32 |
| C | HOH630 |
| site_id | DC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE UNX C 542 |
| Chain | Residue |
| C | THR328 |
| C | MET360 |
| C | LEU361 |
| C | SER362 |
| C | HOH565 |
| site_id | DC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 D 532 |
| Chain | Residue |
| D | THR432 |
| D | LYS433 |
| D | SER434 |
| D | ARG436 |
| D | TYR437 |
| D | PHE521 |
| D | HOH623 |
| site_id | DC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 D 533 |
| Chain | Residue |
| D | HIS78 |
| D | GLY79 |
| site_id | DC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 D 534 |
| Chain | Residue |
| D | ARG436 |
| D | HIS439 |
| site_id | DC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 D 535 |
| Chain | Residue |
| D | HIS274 |
| D | GLU275 |
| D | ARG278 |
| site_id | DC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE UNX D 536 |
| Chain | Residue |
| D | GLU272 |
| D | ASP296 |
| D | UNX537 |
| site_id | EC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE UNX D 537 |
| Chain | Residue |
| D | UNX536 |
| D | UNX538 |
| site_id | EC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE UNX D 538 |
| Chain | Residue |
| D | ASN75 |
| D | SER77 |
| D | ASP113 |
| D | THR114 |
| D | SER243 |
| D | LYS270 |
| D | UNX537 |
| site_id | EC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE UNX D 539 |
| Chain | Residue |
| D | GLU260 |
| D | LYS261 |
| site_id | EC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE UNX D 540 |
| Chain | Residue |
| D | LEU394 |
| D | GLU397 |
| site_id | EC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE UNX D 541 |
| Chain | Residue |
| D | ARG92 |
| D | ASP236 |
| D | ASP238 |
| D | ARG461 |
| site_id | EC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE UNX D 542 |
| Chain | Residue |
| D | PRO53 |
| D | ARG56 |
| D | SER57 |
| site_id | EC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE UNX D 543 |
| Chain | Residue |
| D | THR432 |
| D | ARG455 |
| D | HOH544 |
| D | HOH545 |
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 | ILE265-VAL277 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:23064226 |
| Chain | Residue | Details |
| A | ASN70 | |
| D | ASN70 | |
| D | ARG106 | |
| D | HIS464 | |
| A | ARG106 | |
| A | HIS464 | |
| B | ASN70 | |
| B | ARG106 | |
| B | HIS464 | |
| C | ASN70 | |
| C | ARG106 | |
| C | HIS464 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 20 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P30613 |
| Chain | Residue | Details |
| A | ARG73 | |
| B | THR328 | |
| C | ARG73 | |
| C | LYS270 | |
| C | GLY295 | |
| C | ASP296 | |
| C | THR328 | |
| D | ARG73 | |
| D | LYS270 | |
| D | GLY295 | |
| D | ASP296 | |
| A | LYS270 | |
| D | THR328 | |
| A | GLY295 | |
| A | ASP296 | |
| A | THR328 | |
| B | ARG73 | |
| B | LYS270 | |
| B | GLY295 | |
| B | ASP296 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 28 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:23530218, ECO:0007744|PDB:4FXF |
| Chain | Residue | Details |
| A | ASN75 | |
| B | ASP113 | |
| B | THR114 | |
| B | ARG120 | |
| B | LYS207 | |
| B | GLU272 | |
| C | ASN75 | |
| C | SER77 | |
| C | ASP113 | |
| C | THR114 | |
| C | ARG120 | |
| A | SER77 | |
| C | LYS207 | |
| C | GLU272 | |
| D | ASN75 | |
| D | SER77 | |
| D | ASP113 | |
| D | THR114 | |
| D | ARG120 | |
| D | LYS207 | |
| D | GLU272 | |
| A | ASP113 | |
| A | THR114 | |
| A | ARG120 | |
| A | LYS207 | |
| A | GLU272 | |
| B | ASN75 | |
| B | SER77 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15996096, ECO:0000269|PubMed:23530218, ECO:0007744|PDB:1T5A, ECO:0007744|PDB:4FXF |
| Chain | Residue | Details |
| A | THR432 | |
| C | TRP482 | |
| C | ARG489 | |
| C | ARG516 | |
| D | THR432 | |
| D | TRP482 | |
| D | ARG489 | |
| D | ARG516 | |
| A | TRP482 | |
| A | ARG489 | |
| A | ARG516 | |
| B | THR432 | |
| B | TRP482 | |
| B | ARG489 | |
| B | ARG516 | |
| C | THR432 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | SITE: Transition state stabilizer => ECO:0000250|UniProtKB:P00549 |
| Chain | Residue | Details |
| A | LYS270 | |
| B | LYS270 | |
| C | LYS270 | |
| D | LYS270 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | SITE: Crucial for phosphotyrosine binding => ECO:0000269|PubMed:27199445 |
| Chain | Residue | Details |
| A | LYS433 | |
| B | LYS433 | |
| C | LYS433 | |
| D | LYS433 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | MOD_RES: N-acetylserine => ECO:0000269|Ref.11, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:25944712 |
| Chain | Residue | Details |
| A | SER2 | |
| B | SER2 | |
| C | SER2 | |
| D | SER2 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | MOD_RES: N6,N6,N6-trimethyllysine => ECO:0007744|PubMed:24129315 |
| Chain | Residue | Details |
| A | LYS3 | |
| B | LYS3 | |
| C | LYS3 | |
| D | LYS3 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| A | SER37 | |
| B | SER37 | |
| C | SER37 | |
| D | SER37 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | THR41 | |
| B | THR41 | |
| C | THR41 | |
| D | THR41 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 8 |
| Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
| Chain | Residue | Details |
| A | LYS62 | |
| A | LYS89 | |
| B | LYS62 | |
| B | LYS89 | |
| C | LYS62 | |
| C | LYS89 | |
| D | LYS62 | |
| D | LYS89 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 8 |
| Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P52480 |
| Chain | Residue | Details |
| A | LYS66 | |
| A | LYS498 | |
| B | LYS66 | |
| B | LYS498 | |
| C | LYS66 | |
| C | LYS498 | |
| D | LYS66 | |
| D | LYS498 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 8 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P11980 |
| Chain | Residue | Details |
| A | SER97 | |
| A | SER100 | |
| B | SER97 | |
| B | SER100 | |
| C | SER97 | |
| C | SER100 | |
| D | SER97 | |
| D | SER100 |
| site_id | SWS_FT_FI14 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15592455, ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | TYR105 | |
| B | TYR105 | |
| C | TYR105 | |
| D | TYR105 |
| site_id | SWS_FT_FI15 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | SER127 | |
| B | SER127 | |
| C | SER127 | |
| D | SER127 |
| site_id | SWS_FT_FI16 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P52480 |
| Chain | Residue | Details |
| A | TYR148 | |
| B | TYR148 | |
| C | TYR148 | |
| D | TYR148 |
| site_id | SWS_FT_FI17 |
| Number of Residues | 8 |
| Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P52480 |
| Chain | Residue | Details |
| A | LYS166 | |
| A | LYS322 | |
| B | LYS166 | |
| B | LYS322 | |
| C | LYS166 | |
| C | LYS322 | |
| D | LYS166 | |
| D | LYS322 |
| site_id | SWS_FT_FI18 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:19690332 |
| Chain | Residue | Details |
| A | TYR175 | |
| B | TYR175 | |
| C | TYR175 | |
| D | TYR175 |
| site_id | SWS_FT_FI19 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:19690332 |
| Chain | Residue | Details |
| A | THR195 | |
| B | THR195 | |
| C | THR195 | |
| D | THR195 |
| site_id | SWS_FT_FI20 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861 |
| Chain | Residue | Details |
| A | LYS266 | |
| B | LYS266 | |
| C | LYS266 | |
| D | LYS266 |
| site_id | SWS_FT_FI21 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P52480 |
| Chain | Residue | Details |
| A | LYS270 | |
| B | LYS270 | |
| C | LYS270 | |
| D | LYS270 |
| site_id | SWS_FT_FI22 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:21700219 |
| Chain | Residue | Details |
| A | LYS305 | |
| B | LYS305 | |
| C | LYS305 | |
| D | LYS305 |
| site_id | SWS_FT_FI23 |
| Number of Residues | 8 |
| Details | MOD_RES: 4-hydroxyproline => ECO:0000269|PubMed:21620138 |
| Chain | Residue | Details |
| A | PRO403 | |
| A | PRO408 | |
| B | PRO403 | |
| B | PRO408 | |
| C | PRO403 | |
| C | PRO408 | |
| D | PRO403 | |
| D | PRO408 |
| site_id | SWS_FT_FI24 |
| Number of Residues | 8 |
| Details | MOD_RES: S-nitrosocysteine => ECO:0000269|PubMed:30487609 |
| Chain | Residue | Details |
| A | CYS423 | |
| A | CYS424 | |
| B | CYS423 | |
| B | CYS424 | |
| C | CYS423 | |
| C | CYS424 | |
| D | CYS423 | |
| D | CYS424 |
| site_id | SWS_FT_FI25 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:24120661, ECO:0000269|PubMed:26787900, ECO:0007744|PubMed:19608861 |
| Chain | Residue | Details |
| A | LYS433 | |
| B | LYS433 | |
| C | LYS433 | |
| D | LYS433 |
| site_id | SWS_FT_FI26 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P52480 |
| Chain | Residue | Details |
| A | LYS475 | |
| B | LYS475 | |
| C | LYS475 | |
| D | LYS475 |
| site_id | SWS_FT_FI27 |
| Number of Residues | 4 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 |
| Chain | Residue | Details |
| A | LYS115 | |
| B | LYS115 | |
| C | LYS115 | |
| D | LYS115 |
| site_id | SWS_FT_FI28 |
| Number of Residues | 12 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733 |
| Chain | Residue | Details |
| D | LYS266 | |
| D | LYS270 | |
| A | LYS266 | |
| A | LYS270 | |
| B | LYS266 | |
| B | LYS270 | |
| C | LYS266 | |
| C | LYS270 |
| site_id | SWS_FT_FI29 |
| Number of Residues | 4 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate => ECO:0007744|PubMed:25114211 |
| Chain | Residue | Details |
| A | LYS166 | |
| B | LYS166 | |
| C | LYS166 | |
| D | LYS166 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1pkn |
| Chain | Residue | Details |
| A | THR328 | |
| A | SER362 | |
| A | GLU364 | |
| A | ARG120 | |
| A | ARG73 | |
| A | LYS270 |
| site_id | CSA2 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1pkn |
| Chain | Residue | Details |
| B | THR328 | |
| B | SER362 | |
| B | GLU364 | |
| B | ARG120 | |
| B | ARG73 | |
| B | LYS270 |
| site_id | CSA3 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1pkn |
| Chain | Residue | Details |
| C | THR328 | |
| C | SER362 | |
| C | GLU364 | |
| C | ARG120 | |
| C | ARG73 | |
| C | LYS270 |
| site_id | CSA4 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1pkn |
| Chain | Residue | Details |
| D | THR328 | |
| D | SER362 | |
| D | GLU364 | |
| D | ARG120 | |
| D | ARG73 | |
| D | LYS270 |
