Structure of PDB 4gyn Chain A

Receptor sequence
>4gynA (length=340) Species: 1409 (Bacillus sp. (in: firmicutes)) [Search protein sequence]
MRHGDISSSHDTVGIAVVNYKMPRLHTKAEVIENAKKIADMVVGMKQGLP
GMDLVVFPEYSTMGIMYDQDEMFATAASIPGEETAIFAEACKKADTWGVF
SLTGEKHEDHPNKAPYNTLVLINNKGEIVQKYRKIIPWCPILGWYPGDTT
YVTEGPKGLKISLIVCDDGNYPEIWRDCAMKGAELIVRCQGYMYPAKEQQ
IMMAKAMAWANNTYVAVANATGFDGVYSYFGHSAIIGFDGRTLGECGTEE
NGIQYAEVSISQIRDFRKNAQSQNHLFKLLHRGYTGLINSGEGDRGVAEC
PFDFYRTWVLDAEKARENVEKITRSTVGTAECPIQGIPNE
3D structure
PDB4gyn The mechanism of the amidases: mutating the glutamate adjacent to the catalytic triad inactivates the enzyme due to substrate mispositioning.
ChainA
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E59 N117 G126 K134 C166 G191
Catalytic site (residue number reindexed from 1) E59 N117 G126 K134 C166 G191
Enzyme Commision number 3.5.1.4: amidase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 CL A K134 P137 W138 K134 P137 W138
Gene Ontology
Molecular Function
GO:0003837 beta-ureidopropionase activity
GO:0004040 amidase activity
GO:0016787 hydrolase activity
GO:0043864 indoleacetamide hydrolase activity
Biological Process
GO:0033396 beta-alanine biosynthetic process via 3-ureidopropionate

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Molecular Function
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Biological Process
External links
PDB RCSB:4gyn, PDBe:4gyn, PDBj:4gyn
PDBsum4gyn
PubMed23946488
UniProtQ9L543|AMIE_BACSP Aliphatic amidase (Gene Name=amiE)

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