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1UGR

Crystal structure of aT109S mutant of Co-type nitrile hydratase

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005515molecular_functionprotein binding
A0005575cellular_componentcellular_component
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
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
ACSO113
AHOH330

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:11700034
ChainResidueDetails
ASER109
ASER112
ACSO113
ATYR114

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Cysteine sulfinic acid (-SO2H) => ECO:0000269|PubMed:11700034
ChainResidueDetails
ASER112

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Cysteine sulfenic acid (-SOH) => ECO:0000269|PubMed:11700034
ChainResidueDetails
ATYR114

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ahj
ChainResidueDetails
ACSD111
ACSO113
ASER112

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1ahj
ChainResidueDetails
ACSD111
ACSO113
ASER112
BARG52

222415

PDB entries from 2024-07-10

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