Structure of PDB 1gq6 Chain B

Receptor sequence

>1gq6B (length=301) Species: 1901 (Streptomyces clavuligerus)

SPRYAQIPTFMRLPHDPQPRGYDVVVIGAPYDGGTSYRPGARFGPQAIRS
ESGLIHGVGIDRGPGTFDLINCVDAGDINLTPFDMNIAIDTAQSHLSGLL
KANAAFLMIGGDHSLTVAALRAVAEQHGPLAVVHLDAHSDTNPAFYGGRY
HHGTPFRHGIDEKLIDPAAMVQIGIRGHNPKPDSLDYARGHGVRVVTADE
FGELGVGGTADLIREKVGQRPVYVSVDIDVVDPAFAPGTGTPAPGGLLSR
EVLALLRCVGDLKPVGFDVMEVSPLYDHGGITSILATEIGAELLYQYARA
H

3D structure

• PDB: 1gq6 Oligomeric Structure of Proclavaminic Acid Amidino Hydrolase: Evolution of a Hydrolytic Enzyme in Clavulanic Acid Biosynthesis
• Chain: B
• Resolution: 1.75 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H121 D144 H146 D148 H160 D235 D237 E279
• Catalytic site (residue number reindexed from 1): H113 D136 H138 D140 H152 D227 D229 E271
• Enzyme Commision number: 3.5.3.22: proclavaminate amidinohydrolase.

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	B	H121 D144 D148 D235	H113 D136 D140 D227
BS02	MN	B	D144 H146 D235 D237	D136 H138 D227 D229

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:0033972 proclavaminate amidinohydrolase activity
• GO:0046872 metal ion binding

Biological Process

• GO:0033050 clavulanic acid biosynthetic process
• GO:0033389 putrescine biosynthetic process from arginine, using agmatinase

External links

• PDB: RCSB:1gq6, PDBe:1gq6, PDBj:1gq6
• PDBsum: 1gq6
• PubMed: 12020346
• UniProt: P0DJQ3|PAH_STRCL Proclavaminate amidinohydrolase (Gene Name=pah)