Structure of PDB 3a6e Chain A Binding Site BS01

Receptor Information

>3a6e Chain A (length=257) Species: 303 (Pseudomonas putida)

KSVFVGELTWKEYEARVAAGDCVLMLPVGALEQHGHHMCMNVDVLLPTAV
CKRVAERIGALVMPGLQYGYKSQQKSGGGNHFPGTTSLDGATLTGTVQDI
IRELARHGARRLVLMNGHYENSMFIVEGIDLALRELRYAGIQDFKVVVLS
YWDFVKDPAVIQQLYPEGFLGFDIEHGGVFETSLMLALYPDLVDLDRVVD
HPPATFPPYDVFPVDPARTPAPGTLSSAKTASREKGELILEVCVQGIADA
IREEFPP

Ligand information

• Ligand ID: MN
• InChI: InChI=1S/Mn/q+2
• InChIKey: WAEMQWOKJMHJLA-UHFFFAOYSA-N
• SMILES:
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Mn+2]
  CACTVS 3.341: [Mn++]
• Formula: Mn
• Name: MANGANESE (II) ION
• DrugBank: DB06757
• PDB chain: 3a6e Chain A Residue 300

Receptor-Ligand Complex Structure

Structure summary

• PDB: 3a6e Substitution of Glu122 by glutamine revealed the function of the second water molecule as a proton donor in the binuclear metal enzyme creatininase
• Resolution: 2.0 Å
• Binding residue (original residue number in PDB): E34 D45 H120
• Binding residue (residue number reindexed from 1): E32 D43 H118
• Annotation score: 1

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.

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:3a6e, PDBe:3a6e, PDBj:3a6e
• PDBsum: 3a6e
• PubMed: 20043918
• UniProt: P83772|CRNA_PSEPU Creatinine amidohydrolase (Gene Name=crnA)