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3IW3

Crystal structure of hyperthermophilic nitrilase

Functional Information from GO Data
ChainGOidnamespacecontents
A0000257molecular_functionnitrilase activity
A0003837molecular_functionbeta-ureidopropionase activity
A0006807biological_processobsolete nitrogen compound metabolic process
A0016787molecular_functionhydrolase activity
A0033388biological_processputrescine biosynthetic process from arginine
A0033396biological_processbeta-alanine biosynthetic process via 3-ureidopropionate
A0050126molecular_functionN-carbamoylputrescine amidase activity
A0080061molecular_functionindole-3-acetonitrile nitrilase activity
B0000257molecular_functionnitrilase activity
B0003837molecular_functionbeta-ureidopropionase activity
B0006807biological_processobsolete nitrogen compound metabolic process
B0016787molecular_functionhydrolase activity
B0033388biological_processputrescine biosynthetic process from arginine
B0033396biological_processbeta-alanine biosynthetic process via 3-ureidopropionate
B0050126molecular_functionN-carbamoylputrescine amidase activity
B0080061molecular_functionindole-3-acetonitrile nitrilase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACY A 263
ChainResidue
ACSD146
ATRP149
ALEU172
AVAL173
AMET174
AHOH320

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACY B 263
ChainResidue
BVAL173
BMET174
BHOH264
BCSD146
BTRP149
BLEU172

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACY A 1432
ChainResidue
ATYR82
AARG105
ALEU136
AHOH274
AHOH371
BGLY137

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A 264
ChainResidue
AMET222
AHOH269
AHOH445
AHOH446

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:21095228
ChainResidueDetails
BGLU42
AGLU42

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:21095228
ChainResidueDetails
ALYS113
BLYS113

site_idSWS_FT_FI3
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU00054, ECO:0000269|PubMed:21095228
ChainResidueDetails
ACSD146
BCSD146

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255
ChainResidueDetails
AVAL173
BVAL173

221051

PDB entries from 2024-06-12

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