1E59
E.coli cofactor-dependent phosphoglycerate mutase complexed with vanadate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004619 | molecular_function | phosphoglycerate mutase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006094 | biological_process | gluconeogenesis |
| A | 0006096 | biological_process | glycolytic process |
| A | 0016868 | molecular_function | intramolecular phosphotransferase activity |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0061621 | biological_process | canonical glycolysis |
| A | 0097216 | molecular_function | guanosine tetraphosphate binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL A 3001 |
| Chain | Residue |
| A | TRP67 |
| A | LYS82 |
| site_id | AC2 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE VO3 A 1001 |
| Chain | Residue |
| A | ARG89 |
| A | TYR91 |
| A | LYS99 |
| A | ARG115 |
| A | ARG116 |
| A | ASN185 |
| A | HOH2009 |
| A | HOH2114 |
| A | HOH2115 |
| A | HOH2116 |
| A | HOH2262 |
| A | HOH2263 |
| A | ARG9 |
| A | ASN16 |
| A | ARG20 |
| A | PHE21 |
| A | THR22 |
| A | GLY23 |
| A | GLU88 |
Functional Information from PROSITE/UniProt
| site_id | PS00175 |
| Number of Residues | 10 |
| Details | PG_MUTASE Phosphoglycerate mutase family phosphohistidine signature. LvRHGEsQwN |
| Chain | Residue | Details |
| A | LEU7-ASN16 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Tele-phosphohistidine intermediate","evidences":[{"source":"HAMAP-Rule","id":"MF_01039","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11038361","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11884145","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_01039","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11038361","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11884145","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01039","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11884145","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01039","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11038361","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11884145","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q3JWH7","evidenceCode":"ECO:0000250"},{"source":"HAMAP-Rule","id":"MF_01039","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Site: {"description":"Transition state stabilizer","evidences":[{"source":"HAMAP-Rule","id":"MF_01039","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11038361","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"18723842","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1qhf |
| Chain | Residue | Details |
| A | ARG61 | |
| A | HIS10 | |
| A | HIS183 | |
| A | GLU88 |
