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4KZF

The mechanism of the amidases: The effect of the mutation E142L in the amidase from Geobacillus pallidus

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 Residues5
DetailsBINDING SITE FOR RESIDUE CL A 401
ChainResidue
ATYR60
ALYS134
ATRP138
ALEU142
ATRP144

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

221051

PDB entries from 2024-06-12

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