2Q4R
Ensemble refinement of the protein crystal structure of human phosphomannomutase 2 (PMM2)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004615 | molecular_function | phosphomannomutase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005654 | cellular_component | nucleoplasm |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006013 | biological_process | mannose metabolic process |
| A | 0006486 | biological_process | protein glycosylation |
| A | 0006487 | biological_process | protein N-linked glycosylation |
| A | 0009298 | biological_process | GDP-mannose biosynthetic process |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0019309 | biological_process | mannose catabolic process |
| A | 0043025 | cellular_component | neuronal cell body |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0061728 | biological_process | GDP-mannose biosynthetic process from mannose |
| A | 0061729 | biological_process | GDP-mannose biosynthetic process from fructose-6-phosphate |
| A | 0141199 | biological_process | GDP-mannose biosynthetic process from glucose |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 300 |
| Chain | Residue |
| A | TYR106 |
| A | LYS109 |
| A | LYS156 |
| A | GLY402 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GLY A 400 |
| Chain | Residue |
| A | ARG21 |
| A | TYR201 |
| A | LYS202 |
| A | ARG225 |
| A | HOH480 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GLY A 401 |
| Chain | Residue |
| A | PHE221 |
| A | THR222 |
| A | ASP223 |
| A | THR226 |
| A | GLY228 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GLY A 402 |
| Chain | Residue |
| A | SER105 |
| A | TYR106 |
| A | LYS109 |
| A | EDO300 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Nucleophile => ECO:0000250|UniProtKB:Q92871 |
| Chain | Residue | Details |
| A | ASP12 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:Q92871 |
| Chain | Residue | Details |
| A | ASP14 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 11 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q92871 |
| Chain | Residue | Details |
| A | ASP12 | |
| A | ASP223 | |
| A | THR226 | |
| A | ASP14 | |
| A | ARG21 | |
| A | ARG123 | |
| A | ARG134 | |
| A | ARG141 | |
| A | SER179 | |
| A | ASP181 | |
| A | PHE221 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P31353 |
| Chain | Residue | Details |
| A | ASP209 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | MOD_RES: N-acetylalanine => ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378 |
| Chain | Residue | Details |
| A | ALA2 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9Z2M7 |
| Chain | Residue | Details |
| A | LYS149 |
