Structure of PDB 1gq6 Chain C

Receptor sequence

>1gq6C (length=292) Species: 1901 (Streptomyces clavuligerus)

SPRYAQIPTFMRLPHDPQPRGYDVVVIGAPYDGGTSYRPGARFGPQAIRS
ESGLIHGVGIDGTFDLINCVDAGDINLTPFDMNIAIDTAQSHLSGLLKAN
AAFLMIGGDHSLTVAALRAVAEQHGPLAVVHLDAHSDTNPAFYGGRYHHG
TPFRHGIDEKLIDPAAMVQIGIRGHLDYARGHGVRVVTADEFGELGVGGT
ADLIREKVGQRPVYVSVDIDVVDPAFAPGTGTPAPGGLLSREVLALLRCV
GDLKPVGFDVMEVSPLYDHGGITSILATEIGAELLYQYARAH

3D structure

• PDB: 1gq6 Oligomeric Structure of Proclavaminic Acid Amidino Hydrolase: Evolution of a Hydrolytic Enzyme in Clavulanic Acid Biosynthesis
• Chain: C
• 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): H110 D133 H135 D137 H149 D218 D220 E262
• 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	C	H121 D144 D148 D235	H110 D133 D137 D218
BS02	MN	C	D144 H146 D235 D237	D133 H135 D218 D220

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)