1RBQ
Human GAR Tfase complex structure with 10-(trifluoroacetyl)-5,10-dideazaacyclic-5,6,7,8-tetrahydrofolic acid
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 |
| D | 0004644 | molecular_function | phosphoribosylglycinamide formyltransferase activity |
| D | 0006189 | biological_process | 'de novo' IMP biosynthetic process |
| D | 0009058 | biological_process | biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PO4 A 521 |
| Chain | Residue |
| A | THR10 |
| A | GLY11 |
| A | SER12 |
| A | ASN13 |
| A | LYS170 |
| A | HOH523 |
| A | HOH527 |
| A | HOH555 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 A 522 |
| Chain | Residue |
| A | ARG168 |
| A | HOH608 |
| A | HOH610 |
| A | LYS157 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PO4 B 621 |
| Chain | Residue |
| B | THR10 |
| B | GLY11 |
| B | SER12 |
| B | ASN13 |
| B | LYS170 |
| B | HOH624 |
| B | HOH632 |
| B | HOH654 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 B 622 |
| Chain | Residue |
| B | LYS157 |
| B | ARG168 |
| B | HOH633 |
| B | HOH711 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PO4 C 721 |
| Chain | Residue |
| C | GLY11 |
| C | SER12 |
| C | ASN13 |
| C | LEU14 |
| C | GLN15 |
| C | ALA16 |
| C | LYS45 |
| C | HIS174 |
| C | HOH749 |
| C | HOH787 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PO4 D 821 |
| Chain | Residue |
| D | GLY11 |
| D | SER12 |
| D | ASN13 |
| D | LEU14 |
| D | GLN15 |
| D | ALA16 |
| D | LYS45 |
| D | HIS174 |
| D | HOH850 |
| D | HOH857 |
| site_id | AC7 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE KEU A 510 |
| Chain | Residue |
| A | ARG64 |
| A | LEU85 |
| A | MET89 |
| A | ARG90 |
| A | ILE91 |
| A | LEU92 |
| A | ASN106 |
| A | HIS108 |
| A | PRO109 |
| A | GLY117 |
| A | SER118 |
| A | VAL139 |
| A | ALA140 |
| A | GLU141 |
| A | ASP142 |
| A | VAL143 |
| A | ASP144 |
| A | HOH530 |
| A | HOH532 |
| A | HOH537 |
| A | HOH543 |
| A | HOH562 |
| A | HOH564 |
| A | HOH574 |
| A | HOH623 |
| site_id | AC8 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE KEU B 610 |
| Chain | Residue |
| B | ARG64 |
| B | LEU85 |
| B | MET89 |
| B | ARG90 |
| B | ILE91 |
| B | LEU92 |
| B | ASN106 |
| B | HIS108 |
| B | PRO109 |
| B | GLY117 |
| B | SER118 |
| B | VAL139 |
| B | ALA140 |
| B | GLU141 |
| B | VAL143 |
| B | ASP144 |
| B | HOH623 |
| B | HOH637 |
| B | HOH646 |
| B | HOH660 |
| B | HOH706 |
| C | HOH750 |
| site_id | AC9 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE KEU C 710 |
| Chain | Residue |
| C | PRO109 |
| C | GLY117 |
| C | SER118 |
| C | VAL139 |
| C | ALA140 |
| C | GLU141 |
| C | VAL143 |
| C | ASP144 |
| C | HOH724 |
| C | ARG64 |
| C | LEU85 |
| C | MET89 |
| C | ARG90 |
| C | ILE91 |
| C | LEU92 |
| C | ASN106 |
| C | HIS108 |
| site_id | BC1 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE KEU D 810 |
| Chain | Residue |
| D | ARG64 |
| D | LEU85 |
| D | MET89 |
| D | ARG90 |
| D | ILE91 |
| D | LEU92 |
| D | VAL97 |
| D | ASN106 |
| D | HIS108 |
| D | PRO109 |
| D | GLY117 |
| D | SER118 |
| D | VAL139 |
| D | ALA140 |
| D | GLU141 |
| D | VAL143 |
| D | ASP144 |
| D | HOH829 |
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 | 4 |
| 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 | 20 |
| 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 | 8 |
| 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 | 28 |
| 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 | 4 |
| 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 | CSA10 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1c2t |
| Chain | Residue | Details |
| B | ASP144 | |
| B | HIS108 |
| site_id | CSA11 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1c2t |
| Chain | Residue | Details |
| C | ASP144 | |
| C | HIS108 |
| site_id | CSA12 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1c2t |
| Chain | Residue | Details |
| D | ASP144 | |
| D | 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 | 4 |
| Details | Annotated By Reference To The Literature 1c2t |
| Chain | Residue | Details |
| D | THR135 | |
| D | ASN106 | |
| D | ASP144 | |
| D | HIS108 |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1c2t |
| Chain | Residue | Details |
| A | ASN106 | |
| A | ASP144 | |
| A | HIS108 |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1c2t |
| Chain | Residue | Details |
| B | ASN106 | |
| B | ASP144 | |
| B | HIS108 |
| site_id | CSA7 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1c2t |
| Chain | Residue | Details |
| C | ASN106 | |
| C | ASP144 | |
| C | HIS108 |
| site_id | CSA8 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1c2t |
| Chain | Residue | Details |
| D | ASN106 | |
| D | ASP144 | |
| D | HIS108 |
| site_id | CSA9 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1c2t |
| Chain | Residue | Details |
| A | ASP144 | |
| A | HIS108 |
