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3WVE

Crystal structure of Nitrile Hydratase mutant bR56K complexed with Trimethylacetonitrile, before photo-activation

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0016829molecular_functionlyase activity
A0018822molecular_functionnitrile hydratase activity
A0046872molecular_functionmetal ion binding
A0046914molecular_functiontransition metal ion binding
A0080109molecular_functionindole-3-acetonitrile nitrile hydratase activity
B0016829molecular_functionlyase activity
B0018822molecular_functionnitrile hydratase activity
B0046914molecular_functiontransition metal ion binding
B0080109molecular_functionindole-3-acetonitrile nitrile hydratase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE A 301
ChainResidue
ACYS109
ACSD112
ASER113
ACSO114
ANO302

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NO A 302
ChainResidue
BTAN301
ACSD112
ASER113
ACSO114
AFE301

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 303
ChainResidue
AHOH519
AHOH520
AHOH521
AHOH522
AHOH523
AHOH524

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 304
ChainResidue
ATHR125
ATRP126
BHOH484

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 305
ChainResidue
AARG54
ATHR191
ALYS192

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 306
ChainResidue
ASER19
ATRP23
BGLU31

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE TAN B 301
ChainResidue
ANO302
BTYR37
BMET40
BTYR72
BTYR76

site_idAC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG B 302
ChainResidue
BHOH459
BHOH515
BHOH523
BHOH538
BHOH538
BHOH539
BHOH564

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 303
ChainResidue
BTHR121
BARG132
BLEU208

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:9586994, ECO:0007744|PDB:2AHJ
ChainResidueDetails
ACYS109
ACSD112
ASER113
ACSO114

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Cysteine sulfinic acid (-SO2H) => ECO:0000269|PubMed:9368004, ECO:0000269|PubMed:9586994
ChainResidueDetails
ACSD112

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Cysteine sulfenic acid (-SOH) => ECO:0000269|PubMed:9586994
ChainResidueDetails
ACSO114

Catalytic Information from CSA
site_idMCSA1
Number of Residues3
DetailsM-CSA 57
ChainResidueDetails
BLYS56electrostatic stabiliser, proton acceptor, proton donor
BTYR72proton acceptor, proton donor
BTYR76increase acidity, increase basicity
ACSO114electrofuge, metal ligand, nucleophile, proton acceptor, proton donor

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PDB entries from 2024-07-31

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