1EJJ
CRYSTAL STRUCTURAL ANALYSIS OF PHOSPHOGLYCERATE MUTASE COCRYSTALLIZED WITH 3-PHOSPHOGLYCERATE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004619 | molecular_function | phosphoglycerate mutase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0006007 | biological_process | glucose catabolic process |
| A | 0006096 | biological_process | glycolytic process |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0030145 | molecular_function | manganese ion binding |
| A | 0030435 | biological_process | sporulation resulting in formation of a cellular spore |
| A | 0043937 | biological_process | regulation of sporulation |
| A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MN A 701 |
| Chain | Residue |
| A | ASP403 |
| A | HIS407 |
| A | HIS462 |
| A | 3PG601 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN A 801 |
| Chain | Residue |
| A | 3PG601 |
| A | ASP12 |
| A | SER62 |
| A | LYS336 |
| A | ASP444 |
| A | HIS445 |
| site_id | AC3 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE 3PG A 601 |
| Chain | Residue |
| A | ASN61 |
| A | SER62 |
| A | HIS123 |
| A | ARG153 |
| A | ASP154 |
| A | ARG185 |
| A | ARG191 |
| A | ARG261 |
| A | ARG264 |
| A | LYS336 |
| A | ASP403 |
| A | HIS407 |
| A | HIS445 |
| A | HIS462 |
| A | MN701 |
| A | MN801 |
| A | HOH1017 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Phosphoserine intermediate","evidences":[{"source":"PubMed","id":"10747010","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10764795","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12729763","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 5 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10747010","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10764795","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 9 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10747010","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10764795","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12729763","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10747010","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12729763","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"HAMAP-Rule","id":"MF_01038","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1o98 |
| Chain | Residue | Details |
| A | SER62 | |
| A | ASP154 | |
| A | ARG261 |
| site_id | MCSA1 |
| Number of Residues | 10 |
| Details | M-CSA 738 |
| Chain | Residue | Details |
| A | ASP12 | metal ligand |
| A | HIS462 | metal ligand |
| A | SER62 | metal ligand, nucleofuge, nucleophile, proton acceptor, proton donor |
| A | ASP154 | proton acceptor, proton donor |
| A | ARG261 | electrostatic stabiliser |
| A | LYS336 | proton acceptor, proton donor |
| A | ASP403 | metal ligand |
| A | HIS407 | metal ligand |
| A | ASP444 | metal ligand |
| A | HIS445 | metal ligand |
