3A8G
Crystal structure of Nitrile Hydratase mutant S113A complexed with Trimethylacetonitrile
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0016829 | molecular_function | lyase activity |
A | 0018822 | molecular_function | nitrile hydratase activity |
A | 0046872 | molecular_function | metal ion binding |
A | 0046914 | molecular_function | transition metal ion binding |
A | 0080109 | molecular_function | indole-3-acetonitrile nitrile hydratase activity |
B | 0016829 | molecular_function | lyase activity |
B | 0018822 | molecular_function | nitrile hydratase activity |
B | 0046914 | molecular_function | transition metal ion binding |
B | 0080109 | molecular_function | indole-3-acetonitrile nitrile hydratase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE FE A 301 |
Chain | Residue |
A | CYS109 |
A | CSD112 |
A | ALA113 |
A | CSO114 |
A | NO207 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NO A 207 |
Chain | Residue |
A | FE301 |
B | TAN213 |
A | CSD112 |
A | ALA113 |
A | CSO114 |
A | HOH239 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MG B 302 |
Chain | Residue |
B | HOH324 |
B | HOH324 |
B | HOH432 |
B | HOH433 |
B | HOH434 |
B | HOH435 |
B | HOH436 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG B 303 |
Chain | Residue |
B | HOH425 |
B | HOH426 |
B | HOH427 |
B | HOH428 |
B | HOH429 |
B | HOH430 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG B 304 |
Chain | Residue |
B | HOH381 |
B | HOH386 |
B | HOH388 |
B | HOH389 |
B | HOH401 |
B | HOH405 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE TAN B 213 |
Chain | Residue |
A | NO207 |
B | TYR37 |
B | MET40 |
B | ARG56 |
B | TYR72 |
B | TYR76 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:9586994, ECO:0007744|PDB:2AHJ |
Chain | Residue | Details |
A | CYS109 | |
A | CSD112 | |
A | ALA113 | |
A | CSO114 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | MOD_RES: Cysteine sulfinic acid (-SO2H) => ECO:0000269|PubMed:9368004, ECO:0000269|PubMed:9586994 |
Chain | Residue | Details |
A | CSD112 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | MOD_RES: Cysteine sulfenic acid (-SOH) => ECO:0000269|PubMed:9586994 |
Chain | Residue | Details |
A | CSO114 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 3 |
Details | M-CSA 57 |
Chain | Residue | Details |
B | ARG56 | electrostatic stabiliser, proton acceptor, proton donor |
B | TYR72 | proton acceptor, proton donor |
B | TYR76 | increase acidity, increase basicity |
A | CSO114 | electrofuge, metal ligand, nucleophile, proton acceptor, proton donor |