Structure of PDB 3a6k Chain E

Receptor sequence
>3a6kE (length=258) Species: 303 (Pseudomonas putida) [Search protein sequence]
KSVFVGELTWKEYEARVAAGDCVLMLPVGALEQHGHHMCMNVDVLLPTAV
CKRVAERIGALVMPGLQYGYKSQQKSGGGNHFPGTTSLDGATLTGTVQDI
IRELARHGARRLVLMNGHYQNSMFIVEGIDLALRELRYAGIQDFKVVVLS
YWDFVKDPAVIQQLYPEGFLGWDIEHGGVFETSLMLALYPDLVDLDRVVD
HPPATFPPYDVFPVDPARTPAPGTLSSAKTASREKGELILEVCVQGIADA
IREEFPPT
3D structure
PDB3a6k Substitution of Glu122 by glutamine revealed the function of the second water molecule as a proton donor in the binuclear metal enzyme creatininase
ChainE
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) E34 H36 D45 H120 Q122 H178 E183
Catalytic site (residue number reindexed from 1) E32 H34 D43 H118 Q120 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 E E34 D45 H120 E32 D43 H118
BS02 ZN E 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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:3a6k, PDBe:3a6k, PDBj:3a6k
PDBsum3a6k
PubMed20043918
UniProtP83772|CRNA_PSEPU Creatinine amidohydrolase (Gene Name=crnA)

[Back to BioLiP]