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2ZPI

Complex of Fe-type nitrile hydratase with tert-butylisonitrile, photo-activated for 440min at 293K

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
ATB0301

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A1602
ChainResidue
AHOH1609
AHOH1610
AHOH1605
AHOH1606
AHOH1607
AHOH1608

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A1603
ChainResidue
AHOH1611
AHOH1612
AHOH1613
AHOH1614

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B1601
ChainResidue
BHOH1790
BHOH1791
BHOH1792
BHOH1793
BHOH1794
BHOH1795

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B1604
ChainResidue
BHOH1796
BHOH1797
BHOH1798
BHOH1799
BHOH1800

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE TB0 A 301
ChainResidue
ACSD112
ASER113
ACSO114
AFE300
AHOH1604
BTYR37

site_idAC7
Number of Residues10
DetailsBINDING SITE FOR RESIDUE TRS B1400
ChainResidue
AGLU139
BGLN11
BPRO137
BASP193
BTHR194
BASP195
BHOH1896
BHOH1909
BHOH1916
BHOH1918

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

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PDB entries from 2024-07-24

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