2F90
Crystal structure of bisphosphoglycerate mutase in complex with 3-phosphoglycerate and AlF4-
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004082 | molecular_function | bisphosphoglycerate mutase activity |
| A | 0004619 | molecular_function | phosphoglycerate mutase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005829 | cellular_component | cytosol |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0006096 | biological_process | glycolytic process |
| A | 0007585 | biological_process | respiratory gaseous exchange by respiratory system |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0016868 | molecular_function | intramolecular phosphotransferase activity |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 1901136 | biological_process | carbohydrate derivative catabolic process |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004082 | molecular_function | bisphosphoglycerate mutase activity |
| B | 0004619 | molecular_function | phosphoglycerate mutase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005829 | cellular_component | cytosol |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0006096 | biological_process | glycolytic process |
| B | 0007585 | biological_process | respiratory gaseous exchange by respiratory system |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0016868 | molecular_function | intramolecular phosphotransferase activity |
| B | 0070062 | cellular_component | extracellular exosome |
| B | 1901136 | biological_process | carbohydrate derivative catabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE ALF A 400 |
| Chain | Residue |
| A | ARG10 |
| A | HOH588 |
| A | HIS11 |
| A | ASN17 |
| A | GLN28 |
| A | ARG62 |
| A | GLU89 |
| A | HIS188 |
| A | GLY189 |
| A | 3PG408 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE ALF B 401 |
| Chain | Residue |
| B | ARG10 |
| B | HIS11 |
| B | ASN17 |
| B | ARG62 |
| B | GLU89 |
| B | HIS188 |
| B | GLY189 |
| B | 3PG409 |
| B | HOH601 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE 3PG A 408 |
| Chain | Residue |
| A | ARG10 |
| A | PHE22 |
| A | CYS23 |
| A | SER24 |
| A | GLU89 |
| A | TYR92 |
| A | ARG100 |
| A | ARG116 |
| A | ARG117 |
| A | ASN190 |
| A | ALF400 |
| A | HOH438 |
| A | HOH448 |
| A | HOH518 |
| site_id | AC4 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE 3PG B 409 |
| Chain | Residue |
| B | PHE22 |
| B | CYS23 |
| B | SER24 |
| B | GLU89 |
| B | TYR92 |
| B | ARG100 |
| B | ARG116 |
| B | ARG117 |
| B | ASN190 |
| B | ALF401 |
| B | HOH415 |
| B | HOH442 |
| B | HOH449 |
Functional Information from PROSITE/UniProt
| site_id | PS00175 |
| Number of Residues | 10 |
| Details | PG_MUTASE Phosphoglycerate mutase family phosphohistidine signature. MlRHGEgAwN |
| Chain | Residue | Details |
| A | MET8-ASN17 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Tele-phosphohistidine intermediate","evidences":[{"source":"PubMed","id":"17052986","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"17052986","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 30 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17052986","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 14 |
| Details | Site: {"description":"Not glycated","evidences":[{"source":"PubMed","id":"9832630","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Site: {"description":"Transition state stabilizer","evidences":[{"source":"PubMed","id":"17052986","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 10 |
| Details | Glycosylation: {"description":"N-linked (Glc) (glycation) lysine; in vitro","evidences":[{"source":"PubMed","id":"9832630","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (Glc) (glycation) lysine","evidences":[{"source":"PubMed","id":"9832630","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 | ARG62 | |
| A | HIS11 | |
| A | GLU89 | |
| A | HIS188 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1qhf |
| Chain | Residue | Details |
| B | ARG62 | |
| B | HIS11 | |
| B | GLU89 | |
| B | HIS188 |
