Structure of PDB 3a6k Chain F Binding Site BS02

Receptor Information

>3a6k Chain F (length=257) Species: 303 (Pseudomonas putida)

SVFVGELTWKEYEARVAAGDCVLMLPVGALEQHGHHMCMNVDVLLPTAVC
KRVAERIGALVMPGLQYGYKSQQKSGGGNHFPGTTSLDGATLTGTVQDII
RELARHGARRLVLMNGHYQNSMFIVEGIDLALRELRYAGIQDFKVVVLSY
WDFVKDPAVIQQLYPEGFLGWDIEHGGVFETSLMLALYPDLVDLDRVVDH
PPATFPPYDVFPVDPARTPAPGTLSSAKTASREKGELILEVCVQGIADAI
REEFPPT

Ligand information

• Ligand ID: ZN
• InChI: InChI=1S/Zn/q+2
• InChIKey: PTFCDOFLOPIGGS-UHFFFAOYSA-N
• SMILES:
  CACTVS 3.341: [Zn++]
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Zn+2]
• Formula: Zn
• Name: ZINC ION
• ChEMBL: CHEMBL1236970
• DrugBank: DB14532
• PDB chain: 3a6k Chain F Residue 301

Receptor-Ligand Complex Structure

Structure summary

• PDB: 3a6k Substitution of Glu122 by glutamine revealed the function of the second water molecule as a proton donor in the binuclear metal enzyme creatininase
• Resolution: 2.2 Å
• Binding residue (original residue number in PDB): H36 D45 E183
• Binding residue (residue number reindexed from 1): H33 D42 E180
• Annotation score: 1

Enzymatic activity

• Catalytic site (original residue number in PDB): E34 H36 D45 H120 Q122 H178 E183
• Catalytic site (residue number reindexed from 1): E31 H33 D42 H117 Q119 H175 E180
• Enzyme Commision number: 3.5.2.10: creatininase.

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:3a6k, PDBe:3a6k, PDBj:3a6k
• PDBsum: 3a6k
• PubMed: 20043918
• UniProt: P83772|CRNA_PSEPU Creatinine amidohydrolase (Gene Name=crnA)