Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004743 | molecular_function | pyruvate kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006096 | biological_process | glycolytic process |
| 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 |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004743 | molecular_function | pyruvate kinase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006096 | biological_process | glycolytic process |
| 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 |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0004743 | molecular_function | pyruvate kinase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006096 | biological_process | glycolytic process |
| 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 |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0004743 | molecular_function | pyruvate kinase activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006096 | biological_process | glycolytic process |
| 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 |
| E | 0000287 | molecular_function | magnesium ion binding |
| E | 0003824 | molecular_function | catalytic activity |
| E | 0004743 | molecular_function | pyruvate kinase activity |
| E | 0005524 | molecular_function | ATP binding |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0006096 | biological_process | glycolytic process |
| 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 |
| F | 0000287 | molecular_function | magnesium ion binding |
| F | 0003824 | molecular_function | catalytic activity |
| F | 0004743 | molecular_function | pyruvate kinase activity |
| F | 0005524 | molecular_function | ATP binding |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0006096 | biological_process | glycolytic process |
| 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 |
| G | 0000287 | molecular_function | magnesium ion binding |
| G | 0003824 | molecular_function | catalytic activity |
| G | 0004743 | molecular_function | pyruvate kinase activity |
| G | 0005524 | molecular_function | ATP binding |
| G | 0005737 | cellular_component | cytoplasm |
| G | 0006096 | biological_process | glycolytic process |
| 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 |
| H | 0000287 | molecular_function | magnesium ion binding |
| H | 0003824 | molecular_function | catalytic activity |
| H | 0004743 | molecular_function | pyruvate kinase activity |
| H | 0005524 | molecular_function | ATP binding |
| H | 0005737 | cellular_component | cytoplasm |
| H | 0006096 | biological_process | glycolytic process |
| 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 3000 |
| Chain | Residue |
| A | SER400 |
| A | ASN401 |
| A | THR402 |
| A | ARG404 |
| A | SER405 |
| A | HOH3237 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 3001 |
| Chain | Residue |
| B | SER400 |
| B | ASN401 |
| B | THR402 |
| B | GLY403 |
| B | ARG404 |
| B | SER405 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 C 3002 |
| Chain | Residue |
| C | SER400 |
| C | ASN401 |
| C | THR402 |
| C | ARG404 |
| C | SER405 |
| C | ALA481 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 D 3003 |
| Chain | Residue |
| D | SER400 |
| D | ASN401 |
| D | THR402 |
| D | GLY403 |
| D | ARG404 |
| D | SER405 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 E 3004 |
| Chain | Residue |
| E | SER400 |
| E | ASN401 |
| E | THR402 |
| E | ARG404 |
| E | SER405 |
| E | ALA481 |
| E | HOH1541 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 F 3005 |
| Chain | Residue |
| F | SER400 |
| F | ASN401 |
| F | THR402 |
| F | ARG404 |
| F | SER405 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 H 3006 |
| Chain | Residue |
| H | SER400 |
| H | ASN401 |
| H | THR402 |
| H | GLY403 |
| H | ARG404 |
| H | SER405 |
| H | ALA481 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 G 3007 |
| Chain | Residue |
| G | SER400 |
| G | THR402 |
| G | ARG404 |
| G | SER405 |
| G | ALA481 |
| G | ASP482 |
| G | HOH2654 |
| G | HOH2773 |
| G | HOH2900 |
| site_id | ADP |
| Number of Residues | 5 |
| Details | ADP SUBSTRATE BINDING SITE, BY ANALOGY WITH OTHER CRYSTAL STRUCTURES |
| Chain | Residue |
| A | ARG49 |
| A | ASN51 |
| A | HIS54 |
| A | ARG90 |
| A | ARG174 |
| site_id | ALL |
| Number of Residues | 7 |
| Details | PUTATIVE ALLOSTERIC EFFECTOR SITE, PARTLY BY ANALOGY WITH OTHER CRYSTAL STRUCTURES |
| Chain | Residue |
| A | SER400 |
| A | THR402 |
| A | ARG404 |
| A | SER405 |
| A | LYS453 |
| A | ARG456 |
| A | HIS480 |
| site_id | DIV |
| Number of Residues | 2 |
| Details | DIVALENT CATION BINDING SITE, BY ANALOGY WITH OTHER CRYSTAL STRUCTURES |
| Chain | Residue |
| A | GLU240 |
| A | ASP264 |
| site_id | MON |
| Number of Residues | 4 |
| Details | MONOVALENT CATION BINDING SITE, BY ANALOGY WITH OTHER CRYSTAL STRUCTURES |
| Chain | Residue |
| A | ASN51 |
| A | SER53 |
| A | ASP83 |
| A | THR84 |
| site_id | PEP |
| Number of Residues | 4 |
| Details | PEP SUBSTRATE BINDING SITE, BY ANALOGY WITH OTHER CRYSTAL STRUCTURES |
| Chain | Residue |
| A | ARG49 |
| A | ARG90 |
| A | LYS238 |
| A | THR296 |
Functional Information from PROSITE/UniProt
| site_id | PS00110 |
| Number of Residues | 13 |
| Details | PYRUVATE_KINASE Pyruvate kinase active site signature. ImIICKIENhQGV |
| Chain | Residue | Details |
| A | ILE233-VAL245 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 72 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | ARG49 | |
| B | ARG49 | |
| B | ASN51 | |
| B | SER53 | |
| B | ASP83 | |
| B | THR84 | |
| B | GLU240 | |
| B | GLY263 | |
| B | ASP264 | |
| B | THR296 | |
| C | ARG49 | |
| A | ASN51 | |
| C | ASN51 | |
| C | SER53 | |
| C | ASP83 | |
| C | THR84 | |
| C | GLU240 | |
| C | GLY263 | |
| C | ASP264 | |
| C | THR296 | |
| D | ARG49 | |
| D | ASN51 | |
| A | SER53 | |
| D | SER53 | |
| D | ASP83 | |
| D | THR84 | |
| D | GLU240 | |
| D | GLY263 | |
| D | ASP264 | |
| D | THR296 | |
| E | ARG49 | |
| E | ASN51 | |
| E | SER53 | |
| A | ASP83 | |
| E | ASP83 | |
| E | THR84 | |
| E | GLU240 | |
| E | GLY263 | |
| E | ASP264 | |
| E | THR296 | |
| F | ARG49 | |
| F | ASN51 | |
| F | SER53 | |
| F | ASP83 | |
| A | THR84 | |
| F | THR84 | |
| F | GLU240 | |
| F | GLY263 | |
| F | ASP264 | |
| F | THR296 | |
| H | ARG49 | |
| H | ASN51 | |
| H | SER53 | |
| H | ASP83 | |
| H | THR84 | |
| A | GLU240 | |
| H | GLU240 | |
| H | GLY263 | |
| H | ASP264 | |
| H | THR296 | |
| G | ARG49 | |
| G | ASN51 | |
| G | SER53 | |
| G | ASP83 | |
| G | THR84 | |
| G | GLU240 | |
| A | GLY263 | |
| G | GLY263 | |
| G | ASP264 | |
| G | THR296 | |
| A | ASP264 | |
| A | THR296 | |
| Chain | Residue | Details |
| A | ARG90 | |
| B | ARG90 | |
| C | ARG90 | |
| D | ARG90 | |
| E | ARG90 | |
| F | ARG90 | |
| H | ARG90 | |
| G | ARG90 | |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | SITE: Transition state stabilizer |
| Chain | Residue | Details |
| A | LYS238 | |
| B | LYS238 | |
| C | LYS238 | |
| D | LYS238 | |
| E | LYS238 | |
| F | LYS238 | |
| H | LYS238 | |
| G | LYS238 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1pkn |
| Chain | Residue | Details |
| A | ARG90 | |
| A | LYS238 | |
| A | ARG49 | |
| A | THR296 | |
| A | GLU332 | |
| A | SER330 | |
| site_id | CSA2 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1pkn |
| Chain | Residue | Details |
| B | ARG90 | |
| B | LYS238 | |
| B | ARG49 | |
| B | THR296 | |
| B | GLU332 | |
| B | SER330 | |
| site_id | CSA3 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1pkn |
| Chain | Residue | Details |
| C | ARG90 | |
| C | LYS238 | |
| C | ARG49 | |
| C | THR296 | |
| C | GLU332 | |
| C | SER330 | |
| site_id | CSA4 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1pkn |
| Chain | Residue | Details |
| D | ARG90 | |
| D | LYS238 | |
| D | ARG49 | |
| D | THR296 | |
| D | GLU332 | |
| D | SER330 | |
| site_id | CSA5 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1pkn |
| Chain | Residue | Details |
| E | ARG90 | |
| E | LYS238 | |
| E | ARG49 | |
| E | THR296 | |
| E | GLU332 | |
| E | SER330 | |
| site_id | CSA6 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1pkn |
| Chain | Residue | Details |
| F | ARG90 | |
| F | LYS238 | |
| F | ARG49 | |
| F | THR296 | |
| F | GLU332 | |
| F | SER330 | |
| site_id | CSA7 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1pkn |
| Chain | Residue | Details |
| H | ARG90 | |
| H | LYS238 | |
| H | ARG49 | |
| H | THR296 | |
| H | GLU332 | |
| H | SER330 | |
| site_id | CSA8 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1pkn |
| Chain | Residue | Details |
| G | ARG90 | |
| G | LYS238 | |
| G | ARG49 | |
| G | THR296 | |
| G | GLU332 | |
| G | SER330 | |
