Structure of PDB 3niq Chain A

Receptor sequence
>3niqA (length=315) Species: 208964 (Pseudomonas aeruginosa PAO1) [Search protein sequence]
DHPQPLDAAEIPRFAGIPTFMRLPAFTDPAALQVGLIGVPWDGGTTNRAG
ARHGPREVRNLSSLMRKVHHVSRIAPYDLVRVGDLGDAPVNPIDLLDSLR
RIEGFYRQVHAAGTLPLSVGGDHLVTLPIFRALGRERPLGMVHFDAHSDT
NDRYFGDNPYTHGTPFRRAIEEGLLDPLRTVQIGIRGSVYSPDDDAFARE
CGIRVIHMEEFVELGVEATLAEARRVVGAGPTYVSFDVDVLDPAFAPGTG
TPEIGGMTSLQAQQLVRGLRGLDLVGADVVEVSPPFDVGGATALVGATMM
FELLCLLAESAARSA
3D structure
PDB3niq Crystal structures of Pseudomonas aeruginosa guanidinobutyrase and guanidinopropionase, members of the ureohydrolase superfamily
ChainA
Resolution2.07 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) H123 D145 H147 D149 H162 D237 D239 E281
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 MN A H126 D148 D152 D240 H123 D145 D149 D237
BS02 MN A D148 H150 D240 D242 D145 H147 D237 D239
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:3niq, PDBe:3niq, PDBj:3niq
PDBsum3niq
PubMed21600989
UniProtQ9I6K2|GPUA_PSEAE Guanidinopropionase (Gene Name=gpuA)

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