Structure of PDB 3rva Chain A Binding Site BS02

Receptor Information
>3rva Chain A (length=445) Species: 28108 (Alteromonas macleodii) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SQHKATYQQHIEELQARTREALQREGLDGLVIHSGQGKRLFLDDNHYPFK
VNPQFKAWVPVIDNPNCWLVVNGVDKPTLIFYRPEDFWHKVPPEPNDFWT
DSFDIKLLQQADAVEKFLPYDKSRFAYVGEYIEVAKALGFDNVNPDRVLH
YLHYQRAYKTDYELDCMREANKLAVAGHKAAEQAFREGKSEFDINLAYAA
ASRQGDNDVPYTSIVALNEHASILHYMQCDTVAPKESRSFLIDAGANYHG
YAADITRTYAQEGVHNSAMFRDLIQAVDKVTLTLVDSLKPGVAYTDIHLL
AHDGIAQILHDTGMVNLTPPEIVEMGITRTFFPHGIGHFLGLQVHDVGGL
VNDDRGTPKPAPDDHPFLRCTRMVEARQVFTIEPGLYFIDSLLRDLKATP
ASKYINWDTIDAYKPFGGIRIEDNIIVHRDKNENMTRDLDLNLEH
Ligand information
Ligand IDMN
InChIInChI=1S/Mn/q+2
InChIKeyWAEMQWOKJMHJLA-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Mn+2]
CACTVS 3.341[Mn++]
FormulaMn
NameMANGANESE (II) ION
ChEMBL
DrugBankDB06757
ZINC
PDB chain3rva Chain A Residue 453 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB3rva Organophosphorus acid anhydrolase from Alteromonas macleodii: structural study and functional relationship to prolidases.
Resolution1.8 Å
Binding residue
(original residue number in PDB)		D255 H339 T382 E384 E423
Binding residue
(residue number reindexed from 1)		D254 H338 T381 E383 E422
Annotation score1
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:3rva, PDBe:3rva, PDBj:3rva
PDBsum3rva
PubMed23545636
UniProtF8UVJ4

[Back to BioLiP]