Structure of PDB 3nip Chain B

Receptor sequence
>3nipB (length=316) Species: 208964 (Pseudomonas aeruginosa PAO1) [Search protein sequence]
NDHPQPLDAAEIPRFAGIPTFMRLPAFTDPAALQVGLIGVPWDGGTTNRA
GARHGPREVRNLSSLMRKVHHVSRIAPYDLVRVGDLGDAPVNPIDLLDSL
RRIEGFYRQVHAAGTLPLSVGGDHLVTLPIFRALGRERPLGMVHFDAHSD
TNDRYFGDNPYTHGTPFRRAIEEGLLDPLRTVQIGIRGSVYSPDDDAFAR
ECGIRVIHMEEFVELGVEATLAEARRVVGAGPTYVSFDVDVLDPAFAPGT
GTPEIGGMTSLQAQQLVRGLRGLDLVGADVVEVSPPFDVGGATALVGATM
MFELLCLLAESAARSA
3D structure
PDB3nip Crystal structures of Pseudomonas aeruginosa guanidinobutyrase and guanidinopropionase, members of the ureohydrolase superfamily
ChainB
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H126 D148 H150 D152 H165 D240 D242 E284
Catalytic site (residue number reindexed from 1) H124 D146 H148 D150 H163 D238 D240 E282
Enzyme Commision number 3.5.3.17: guanidinopropionase.
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 16D B R51 P246 P250 R49 P244 P248
BS02 16D B F248 A294 V298 F246 A292 V296
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:0047972 guanidinopropionase activity
Biological 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:3nip, PDBe:3nip, PDBj:3nip
PDBsum3nip
PubMed21600989
UniProtQ9I6K2|GPUA_PSEAE Guanidinopropionase (Gene Name=gpuA)

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