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4GYL

The E142L mutant of the amidase from Geobacillus pallidus showing the result of Michael addition of acrylamide at the active site cysteine

Functional Information from GO Data
ChainGOidnamespacecontents
A0003837molecular_functionbeta-ureidopropionase activity
A0004040molecular_functionamidase activity
A0006807biological_processobsolete nitrogen compound metabolic process
A0016787molecular_functionhydrolase activity
A0033396biological_processbeta-alanine biosynthetic process via 3-ureidopropionate
A0043864molecular_functionindoleacetamide hydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE ROP A 401
ChainResidue
AGLU59
ATYR60
ALYS134
ATRP138
ALEU142
ACYS166
AASP167
AGLY191
ACL402

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CL A 402
ChainResidue
ATYR60
ALYS134
ATRP138
ALEU142
ATRP144
AROP401

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000250
ChainResidueDetails
AGLU59

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000250
ChainResidueDetails
ALYS134

site_idSWS_FT_FI3
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000250
ChainResidueDetails
ACYS166

219140

PDB entries from 2024-05-01

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