Structure of PDB 1v7z Chain A

Receptor sequence

>1v7zA (length=257) Species: 306 (Pseudomonas sp.)

KSVFVGELTWKEYEARVAAGDCVLMLPVGALEQHGHHMCMNVDVLLPTAV
CKRVAERIGALVMPGLQYGYKSQQKSGGGNHFPGTTSLDGATLTGTVQDI
IRELARHGARRLVLMNGHYENSMFIVEGIDLALRELRYAGIQDFKVVVLS
YWDFVKDPAVIQQLYPEGFLGWDIEHGGVFETSLMLALYPDLVDLDRVVD
HPPATFPPYDVFPVDPARTPAPGTLSSAKTASREKGELILEVCVQGIADA
IREEFPP

3D structure

• PDB: 1v7z Crystal structures of creatininase reveal the substrate binding site and provide an insight into the catalytic mechanism
• Chain: A
• Resolution: 1.6 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): E34 H36 D45 H120 E122 H178 E183
• Catalytic site (residue number reindexed from 1): E32 H34 D43 H118 E120 H176 E181
• Enzyme Commision number: 3.5.2.10: creatininase.

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	E34 D45 H120	E32 D43 H118
BS02	ZN	A	H36 D45 E183	H34 D43 E181
BS03	CRN	A	D45 S78 H120 Y121 W154 W174 D175 E177 H178 E183	D43 S76 H118 Y119 W152 W172 D173 E175 H176 E181

Gene Ontology

Molecular Function

• GO:0008270 zinc ion binding
• GO:0016787 hydrolase activity
• GO:0016811 hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
• GO:0030145 manganese ion binding
• GO:0046872 metal ion binding
• GO:0047789 creatininase activity

Biological Process

• GO:0006601 creatine biosynthetic process
• GO:0006602 creatinine catabolic process
• GO:0009231 riboflavin biosynthetic process

External links

• PDB: RCSB:1v7z, PDBe:1v7z, PDBj:1v7z
• PDBsum: 1v7z
• PubMed: 15003455
• UniProt: P83772|CRNA_PSEPU Creatinine amidohydrolase (Gene Name=crnA)