1T3Z
Formyl-CoA Tranferase mutant Asp169 to Ser
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0008410 | molecular_function | CoA-transferase activity |
A | 0016740 | molecular_function | transferase activity |
A | 0033608 | molecular_function | formyl-CoA transferase activity |
A | 0033611 | biological_process | oxalate catabolic process |
B | 0003824 | molecular_function | catalytic activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0008410 | molecular_function | CoA-transferase activity |
B | 0016740 | molecular_function | transferase activity |
B | 0033608 | molecular_function | formyl-CoA transferase activity |
B | 0033611 | biological_process | oxalate catabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE CAO A 429 |
Chain | Residue |
A | HIS15 |
A | PHE97 |
A | GLY98 |
A | ALA101 |
A | ARG104 |
A | MET105 |
A | VAL124 |
A | LYS137 |
A | VAL138 |
A | TYR139 |
A | GLU140 |
A | VAL16 |
A | MET200 |
A | HOH618 |
B | ASN287 |
A | GLN17 |
A | ALA18 |
A | ARG38 |
A | LEU72 |
A | MET74 |
A | LYS75 |
A | ASN96 |
site_id | AC2 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE CAO B 1429 |
Chain | Residue |
A | LYS52 |
B | HIS15 |
B | VAL16 |
B | ARG38 |
B | LEU72 |
B | MET74 |
B | LYS75 |
B | ASN96 |
B | PHE97 |
B | GLY98 |
B | ALA101 |
B | ARG104 |
B | MET105 |
B | VAL124 |
B | LYS137 |
B | VAL138 |
B | GLU140 |
B | SER169 |
B | MET200 |
B | HOH1535 |
B | HOH1537 |
B | HOH1592 |
B | HOH1595 |
B | HOH1606 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | Active site: {"description":"Nucleophile","evidences":[{"source":"HAMAP-Rule","id":"MF_00742","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15213226","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 26 |
Details | Binding site: {} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00742","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12839984","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15213226","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18162462","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1xvt |
Chain | Residue | Details |
A | SER169 |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1xvt |
Chain | Residue | Details |
B | SER169 |
site_id | MCSA1 |
Number of Residues | 5 |
Details | M-CSA 155 |
Chain | Residue | Details |
A | GLN17 | electrostatic stabiliser, hydrogen bond donor |
A | GLU140 | electrostatic stabiliser, hydrogen bond donor |
A | SER169 | covalently attached, electrofuge, electrophile, nucleofuge, nucleophile |
A | GLY260 | electrostatic stabiliser, hydrogen bond acceptor |
A | GLY261 | electrostatic stabiliser, hydrogen bond donor |
site_id | MCSA2 |
Number of Residues | 5 |
Details | M-CSA 155 |
Chain | Residue | Details |
B | GLN17 | electrostatic stabiliser, hydrogen bond donor |
B | GLU140 | electrostatic stabiliser, hydrogen bond donor |
B | SER169 | covalently attached, electrofuge, electrophile, nucleofuge, nucleophile |
B | GLY260 | electrostatic stabiliser, hydrogen bond acceptor |
B | GLY261 | electrostatic stabiliser, hydrogen bond donor |