Structure of PDB 3a6h Chain D

Receptor sequence
>3a6hD (length=257) Species: 303 (Pseudomonas putida) [Search protein sequence]
KSVFVGELTWKEYEARVAAGDCVLMLPVGALEQHGHHMCMNVDVLLPTAV
CKRVAERIGALVMPGLQYGYKSQQKSGGGNHFPGTTSLDGATLTGTVQDI
IRELARHGARRLVLMNGHYENSMFIVEGIDLALRELRYAGIQDFKVVVLS
YADFVKDPAVIQQLYPEGFLGWDIEHGGVFETSLMLALYPDLVDLDRVVD
HPPATFPPYDVFPVDPARTPAPGTLSSAKTASREKGELILEVCVQGIADA
IREEFPP
3D structure
PDB3a6h Substitution of Glu122 by glutamine revealed the function of the second water molecule as a proton donor in the binuclear metal enzyme creatininase
ChainD
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 D E34 D45 H120 E32 D43 H118
BS02 ZN D H36 D45 E183 H34 D43 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

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Molecular Function
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Biological Process
External links
PDB RCSB:3a6h, PDBe:3a6h, PDBj:3a6h
PDBsum3a6h
PubMed20043918
UniProtP83772|CRNA_PSEPU Creatinine amidohydrolase (Gene Name=crnA)

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