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4OB0

Crystal Structure of Nitrile Hydratase from Pseudonocardia thermophila bound to Phenyl Boronic Acid

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005515molecular_functionprotein binding
A0005575cellular_componentcellular_component
A0006807biological_processobsolete nitrogen compound metabolic process
A0016829molecular_functionlyase activity
A0018822molecular_functionnitrile hydratase activity
A0046872molecular_functionmetal ion binding
A0046914molecular_functiontransition metal ion binding
A0050897molecular_functioncobalt ion binding
A0050899biological_processnitrile catabolic process
A0080109molecular_functionindole-3-acetonitrile nitrile hydratase activity
B0005515molecular_functionprotein binding
B0005575cellular_componentcellular_component
B0006807biological_processobsolete nitrogen compound metabolic process
B0016829molecular_functionlyase activity
B0018822molecular_functionnitrile hydratase activity
B0046914molecular_functiontransition metal ion binding
B0050899biological_processnitrile catabolic process
B0080109molecular_functionindole-3-acetonitrile nitrile hydratase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CO A 301
ChainResidue
ACYS108
ACSD111
ASER112
ACYS113
APBC302

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PBC A 302
ChainResidue
AARG167
ACO301
BPHE51
BARG52
BTRP72
AGLN89
ACSD111
ASER112
ACYS113

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:11700034
ChainResidueDetails
ACYS108
ACSD111
ASER112
ACYS113

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Cysteine sulfinic acid (-SO2H) => ECO:0000269|PubMed:11700034
ChainResidueDetails
ACSD111

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Cysteine sulfenic acid (-SOH) => ECO:0000269|PubMed:11700034
ChainResidueDetails
ACYS113

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PDB entries from 2024-05-01

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