Structure of PDB 3nio Chain D

Receptor sequence
>3nioD (length=316) Species: 208964 (Pseudomonas aeruginosa PAO1) [Search protein sequence]
NLHQPLGGNEMPRFGGIATMMRLPHVQSPAELDALDAAFVGVPLDIGTSL
RSGTRFGPREIRAESVMIRPYNMATGAAPFDSLNVADIGDVAINTFNLLE
AVRIIEQEYDRILGHGILPLTLGGDHTITLPILRAIKKKHGKVGLVHVDA
HADVNDHMFGEKIAHGTTFRRAVEEDLLDCDRVVQIGLRAQGYTAEDFNW
SRKQGFRVVQAEECWHKSLEPLMAEVREKVGGGPVYLSFDIDGIDPAWAP
GTGTPEIGGLTTIQAMEIIRGCQGLDLIGCDLVEVSPPYDTTGNTSLLGA
NLLYEMLCVLPGVVRR
3D structure
PDB3nio Crystal structures of Pseudomonas aeruginosa guanidinobutyrase and guanidinopropionase, members of the ureohydrolase superfamily
ChainD
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H129 D152 H154 D156 H168 D243 D245 E287
Catalytic site (residue number reindexed from 1) H126 D149 H151 D153 H165 D240 D242 E284
Enzyme Commision number 3.5.3.7: guanidinobutyrase.
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 MN D H129 D152 D156 D243 H126 D149 D153 D240
BS02 MN D D152 H154 D243 D245 D149 H151 D240 D242
Gene Ontology
Molecular Function
GO:0008783 agmatinase activity
GO:0016787 hydrolase activity
GO:0016813 hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
GO:0046872 metal ion binding
GO:0047971 guanidinobutyrase activity
Biological Process
GO:0006527 arginine catabolic process
GO:0033389 putrescine biosynthetic process from arginine, using agmatinase

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Molecular Function
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Biological Process
External links
PDB RCSB:3nio, PDBe:3nio, PDBj:3nio
PDBsum3nio
PubMed21600989
UniProtQ9I3S3|GBUA_PSEAE Guanidinobutyrase (Gene Name=gbuA)

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