Structure of PDB 1j2t Chain D

Receptor sequence
>1j2tD (length=257) Species: 303 (Pseudomonas putida) [Search protein sequence]
KSVFVGELTWKEYEARVAAGDCVLMLPVGALEQHGHHMCMNVDVLLPTAV
CKRVAERIGALVMPGLQYGYKSQQKSGGGNHFPGTTSLDGATLTGTVQDI
IRELARHGARRLVLMNGHYENSMFIVEGIDLALRELRYAGIQDFKVVVLS
YWDFVKDPAVIQQLYPEGFLGWDIEHGGVFETSLMLALYPDLVDLDRVVD
HPPATFPPYDVFPVDPARTPAPGTLSSAKTASREKGELILEVCVQGIADA
IREEFPP
3D structure
PDB1j2t Crystal structures of creatininase reveal the substrate binding site and provide an insight into the catalytic mechanism
ChainD
Resolution1.8 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 ZN D H36 D45 E183 H34 D43 E181
BS02 MN D E34 D45 H120 E32 D43 H118
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
View graph for
Biological Process
External links
PDB RCSB:1j2t, PDBe:1j2t, PDBj:1j2t
PDBsum1j2t
PubMed15003455
UniProtP83772|CRNA_PSEPU Creatinine amidohydrolase (Gene Name=crnA)

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