Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

2ZPB

nitrosylated Fe-type nitrile hydratase

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 300
ChainResidue
ACYS109
ACSD112
ASER113
ACSO114
ANO301

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NO A 301
ChainResidue
AHOH1349
ACSD112
ASER113
ACSO114
AFE300

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A1302
ChainResidue
AHOH1384
AHOH1466
AHOH1476
AHOH1510
AHOH1525
AHOH1557

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG A1303
ChainResidue
AHOH1374
AHOH1411
AHOH1549
AHOH1559
AHOH1574
AHOH1582
BGLU119

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B1301
ChainResidue
BHOH1321
BHOH1390
BHOH1392
BHOH1399
BHOH1405
BHOH1435

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_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ahj
ChainResidueDetails
BARG56

site_idMCSA1
Number of Residues3
DetailsM-CSA 57
ChainResidueDetails
BARG56electrostatic stabiliser, proton acceptor, proton donor
BTYR72proton acceptor, proton donor
BTYR76increase acidity, increase basicity
ACSO114electrofuge, metal ligand, nucleophile, proton acceptor, proton donor

222926

PDB entries from 2024-07-24

PDB statisticsPDBj update infoContact PDBjnumon