2AHJ
NITRILE HYDRATASE COMPLEXED WITH NITRIC OXIDE
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0006807 | biological_process | obsolete nitrogen compound metabolic process |
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 | 0006807 | biological_process | obsolete nitrogen compound metabolic process |
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 |
C | 0003824 | molecular_function | catalytic activity |
C | 0006807 | biological_process | obsolete nitrogen compound metabolic process |
C | 0016829 | molecular_function | lyase activity |
C | 0018822 | molecular_function | nitrile hydratase activity |
C | 0046872 | molecular_function | metal ion binding |
C | 0046914 | molecular_function | transition metal ion binding |
C | 0080109 | molecular_function | indole-3-acetonitrile nitrile hydratase activity |
D | 0006807 | biological_process | obsolete nitrogen compound metabolic process |
D | 0016829 | molecular_function | lyase activity |
D | 0018822 | molecular_function | nitrile hydratase activity |
D | 0046914 | molecular_function | transition metal ion binding |
D | 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 300 |
Chain | Residue |
A | CSD112 |
A | SER113 |
A | CSO114 |
A | NO301 |
A | CYS109 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN C 303 |
Chain | Residue |
B | HIS29 |
C | HIS6 |
C | HOH394 |
D | GLU31 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE FE C 300 |
Chain | Residue |
C | CYS109 |
C | CSD112 |
C | SER113 |
C | CSO114 |
C | NO301 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN A 303 |
Chain | Residue |
A | HIS6 |
A | HOH387 |
A | HOH460 |
B | GLU31 |
D | HIS29 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 D 304 |
Chain | Residue |
B | ARG107 |
D | GLY14 |
D | LYS15 |
D | HOH461 |
D | HOH462 |
D | HOH486 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 A 305 |
Chain | Residue |
A | SER182 |
A | GLN183 |
D | ARG128 |
D | THR152 |
D | HOH309 |
D | HOH414 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 B 306 |
Chain | Residue |
B | GLY14 |
B | LYS15 |
B | HOH410 |
D | ARG107 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NO A 301 |
Chain | Residue |
A | CSD112 |
A | SER113 |
A | CSO114 |
A | FE300 |
B | DIO302 |
site_id | AC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE DIO B 302 |
Chain | Residue |
A | TRP117 |
A | NO301 |
B | TYR37 |
B | VAL52 |
B | ARG56 |
B | TYR76 |
site_id | BC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NO C 301 |
Chain | Residue |
C | CSD112 |
C | SER113 |
C | CSO114 |
C | FE300 |
D | DIO302 |
site_id | BC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE DIO D 302 |
Chain | Residue |
C | NO301 |
D | TYR37 |
D | VAL52 |
D | TYR76 |
site_id | CTA |
Number of Residues | 4 |
Details | NON-HEME IRON CENTER AND CATALYTIC SITE IN CHAIN A |
Chain | Residue |
A | CYS109 |
A | CSD112 |
A | SER113 |
A | CSO114 |
site_id | CTB |
Number of Residues | 4 |
Details | NON-HEME IRON CENTER AND CATALYTIC SITE IN CHAIN C |
Chain | Residue |
C | CYS109 |
C | CSD112 |
C | SER113 |
C | CSO114 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:9586994, ECO:0007744|PDB:2AHJ |
Chain | Residue | Details |
A | SER110 | |
A | SER113 | |
A | CSO114 | |
A | THR115 | |
C | SER110 | |
C | SER113 | |
C | CSO114 | |
C | THR115 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | MOD_RES: Cysteine sulfinic acid (-SO2H) => ECO:0000269|PubMed:9368004, ECO:0000269|PubMed:9586994 |
Chain | Residue | Details |
A | SER113 | |
C | SER113 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: Cysteine sulfenic acid (-SOH) => ECO:0000269|PubMed:9586994 |
Chain | Residue | Details |
A | THR115 | |
C | THR115 |
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 | THR115 | electrofuge, metal ligand, nucleophile, proton acceptor, proton donor |
site_id | MCSA2 |
Number of Residues | 3 |
Details | M-CSA 57 |
Chain | Residue | Details |
D | ARG56 | electrostatic stabiliser, proton acceptor, proton donor |
D | TYR72 | proton acceptor, proton donor |
D | TYR76 | increase acidity, increase basicity |
C | THR115 | electrofuge, metal ligand, nucleophile, proton acceptor, proton donor |