Structure of PDB 3rva Chain A Binding Site BS01

Receptor Information

>3rva Chain A (length=445) Species: 28108 (Alteromonas macleodii)

SQHKATYQQHIEELQARTREALQREGLDGLVIHSGQGKRLFLDDNHYPFK
VNPQFKAWVPVIDNPNCWLVVNGVDKPTLIFYRPEDFWHKVPPEPNDFWT
DSFDIKLLQQADAVEKFLPYDKSRFAYVGEYIEVAKALGFDNVNPDRVLH
YLHYQRAYKTDYELDCMREANKLAVAGHKAAEQAFREGKSEFDINLAYAA
ASRQGDNDVPYTSIVALNEHASILHYMQCDTVAPKESRSFLIDAGANYHG
YAADITRTYAQEGVHNSAMFRDLIQAVDKVTLTLVDSLKPGVAYTDIHLL
AHDGIAQILHDTGMVNLTPPEIVEMGITRTFFPHGIGHFLGLQVHDVGGL
VNDDRGTPKPAPDDHPFLRCTRMVEARQVFTIEPGLYFIDSLLRDLKATP
ASKYINWDTIDAYKPFGGIRIEDNIIVHRDKNENMTRDLDLNLEH

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: 3rva Chain A Residue 452

Receptor-Ligand Complex Structure

Structure summary

• PDB: 3rva Organophosphorus acid anhydrolase from Alteromonas macleodii: structural study and functional relationship to prolidases.
• Resolution: 1.8 Å
• Binding residue (original residue number in PDB): D244 D255 E423
• Binding residue (residue number reindexed from 1): D243 D254 E422
• Annotation score: 1

Enzymatic activity

• Catalytic site (original residue number in PDB): D45 H226 D244 D255 H335 H339 H346 E384 Y388 R421 E423
• Catalytic site (residue number reindexed from 1): D44 H225 D243 D254 H334 H338 H345 E383 Y387 R420 E422
• Enzyme Commision number: 3.4.13.9: Xaa-Pro dipeptidase.

Gene Ontology

Molecular Function

• GO:0004177 aminopeptidase activity
• GO:0008235 metalloexopeptidase activity
• GO:0008237 metallopeptidase activity
• GO:0016795 phosphoric triester hydrolase activity
• GO:0016805 dipeptidase activity
• GO:0046872 metal ion binding
• GO:0102009 proline dipeptidase activity

Biological Process

• GO:0006508 proteolysis

Cellular Component

• GO:0005829 cytosol

External links

• PDB: RCSB:3rva, PDBe:3rva, PDBj:3rva
• PDBsum: 3rva
• PubMed: 23545636
• UniProt: F8UVJ4