5UE7
Crystal structure of the phosphomannomutase PMM1 from Candida albicans, apoenzyme state
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004615 | molecular_function | phosphomannomutase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006013 | biological_process | mannose metabolic process |
| A | 0006487 | biological_process | protein N-linked glycosylation |
| A | 0009298 | biological_process | GDP-mannose biosynthetic process |
| A | 0016020 | cellular_component | membrane |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0062040 | cellular_component | fungal biofilm matrix |
| A | 0180047 | biological_process | dolichol phosphate mannose biosynthetic process |
| B | 0004615 | molecular_function | phosphomannomutase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006013 | biological_process | mannose metabolic process |
| B | 0006487 | biological_process | protein N-linked glycosylation |
| B | 0009298 | biological_process | GDP-mannose biosynthetic process |
| B | 0016020 | cellular_component | membrane |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0062040 | cellular_component | fungal biofilm matrix |
| B | 0180047 | biological_process | dolichol phosphate mannose biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 301 |
| Chain | Residue |
| A | ASP16 |
| A | ASP18 |
| A | ASP213 |
| A | HOH417 |
| A | HOH437 |
| A | HOH470 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 302 |
| Chain | Residue |
| A | THR230 |
| B | GLU247 |
| B | HOH425 |
| A | TYR225 |
| A | ASN226 |
| A | ASP227 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue CL A 303 |
| Chain | Residue |
| A | PHE123 |
| A | ILE124 |
| B | PHE123 |
| B | ILE124 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 301 |
| Chain | Residue |
| B | ASP16 |
| B | ASP18 |
| B | ASP213 |
| B | HOH402 |
| B | HOH428 |
| B | HOH530 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 302 |
| Chain | Residue |
| A | GLU247 |
| A | HOH408 |
| B | TYR225 |
| B | ASP227 |
| B | THR230 |
| B | HOH528 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"UniProtKB","id":"Q92871","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"UniProtKB","id":"Q92871","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2016","submissionDatabase":"PDB data bank","title":"Crystal structure of the phosphomannomutase PMM1 from Candida albicans, apoenzyme state.","authors":["Stogios P.J."]}},{"source":"PDB","id":"5UE7","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q92871","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
