1MEN
complex structure of human GAR Tfase and substrate beta-GAR
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004644 | molecular_function | phosphoribosylglycinamide formyltransferase activity |
| A | 0006189 | biological_process | 'de novo' IMP biosynthetic process |
| A | 0009058 | biological_process | biosynthetic process |
| B | 0004644 | molecular_function | phosphoribosylglycinamide formyltransferase activity |
| B | 0006189 | biological_process | 'de novo' IMP biosynthetic process |
| B | 0009058 | biological_process | biosynthetic process |
| C | 0004644 | molecular_function | phosphoribosylglycinamide formyltransferase activity |
| C | 0006189 | biological_process | 'de novo' IMP biosynthetic process |
| C | 0009058 | biological_process | biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE GAR A 223 |
| Chain | Residue |
| A | THR10 |
| A | HOH231 |
| A | HOH235 |
| A | HOH264 |
| A | GLY11 |
| A | SER12 |
| A | ASN13 |
| A | MET89 |
| A | PRO109 |
| A | LYS170 |
| A | GLU173 |
| A | HOH225 |
| site_id | AC2 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE GAR B 224 |
| Chain | Residue |
| B | THR10 |
| B | GLY11 |
| B | SER12 |
| B | ASN13 |
| B | GLY87 |
| B | MET89 |
| B | PRO109 |
| B | LYS170 |
| B | GLU173 |
| B | HOH225 |
| B | HOH226 |
| B | HOH229 |
| B | HOH235 |
| B | HOH239 |
| B | HOH244 |
| site_id | AC3 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE GAR C 225 |
| Chain | Residue |
| C | THR10 |
| C | GLY11 |
| C | SER12 |
| C | ASN13 |
| C | GLY87 |
| C | MET89 |
| C | ILE107 |
| C | PRO109 |
| C | LYS170 |
| C | GLU173 |
| C | HOH226 |
| C | HOH232 |
| C | HOH233 |
| C | HOH241 |
| C | HOH251 |
Functional Information from PROSITE/UniProt
| site_id | PS00373 |
| Number of Residues | 24 |
| Details | GART Phosphoribosylglycinamide formyltransferase active site. GcTVhFVaEdVDaGqiIlqeavpV |
| Chain | Residue | Details |
| A | GLY133-VAL156 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"P08179","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 15 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12450384","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16026156","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1MEN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1ZLY","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12755606","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1NJS","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 21 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12755606","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"16026156","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1NJS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1ZLY","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | Site: {"description":"Raises pKa of active site His","evidences":[{"source":"UniProtKB","id":"P08179","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1c2t |
| Chain | Residue | Details |
| A | THR135 | |
| A | ASN106 | |
| A | ASP144 | |
| A | HIS108 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1c2t |
| Chain | Residue | Details |
| B | THR135 | |
| B | ASN106 | |
| B | ASP144 | |
| B | HIS108 |
| site_id | CSA3 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1c2t |
| Chain | Residue | Details |
| C | THR135 | |
| C | ASN106 | |
| C | ASP144 | |
| C | HIS108 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1c2t |
| Chain | Residue | Details |
| A | ASN106 | |
| A | ASP144 | |
| A | HIS108 |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1c2t |
| Chain | Residue | Details |
| B | ASN106 | |
| B | ASP144 | |
| B | HIS108 |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1c2t |
| Chain | Residue | Details |
| C | ASN106 | |
| C | ASP144 | |
| C | HIS108 |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1c2t |
| Chain | Residue | Details |
| A | ASP144 | |
| A | HIS108 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1c2t |
| Chain | Residue | Details |
| B | ASP144 | |
| B | HIS108 |
| site_id | CSA9 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1c2t |
| Chain | Residue | Details |
| C | ASP144 | |
| C | HIS108 |
