Structure of PDB 3l24 Chain C Binding Site BS01

Receptor Information
>3l24 Chain C (length=417) Species: 232 (Alteromonas sp.) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MNKLAVLYAEHIATLQKRTREIIERENLDGVVFHSGQAKRQFLDDMYYPF
KVNPQFKAWLPVIDNPHCWIVANGTDKPKLIFYRPVDFWHKVPDEPNEYW
ADYFDIELLVKPDQVEKLLPYDKARFAYIGEYLEVAQALGFELMNPEPVM
NFYHYHRAYKTQYELACMREANKIAVQGHKAARDAFFQGKSEFEIQQAYL
LATQHSENDNPYGNIVALNENCAILHYTHFDRVAPATHRSFLIDAGANFN
GYAADITRTYDFTGEGEFAELVATMKQHQIALMNQLAPGKLYGELHLDCH
QRVAQTLSDFNIVDLSADEIVAKGITSTFFPHGLGHHIGLQVHDVTRKIE
ANQVFTIEPGLYFIDSLLGDLAATDNNQHINWDKVAELKPFGGIRIEDNI
IVHEDSLENMTRELRLR
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 chain3l24 Chain C Residue 518 [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]
PDB3l24 Structural insights into the dual activities of the nerve agent degrading organophosphate anhydrolase/prolidase.
Resolution2.3 Å
Binding residue
(original residue number in PDB)		D255 H336 E381 E420
Binding residue
(residue number reindexed from 1)		D255 H336 E358 E397
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) D45 H226 D244 D255 H332 H336 H343 E381 Y385 R418 E420
Catalytic site (residue number reindexed from 1) D45 H226 D244 D255 H332 H336 H343 E358 Y362 R395 E397
Enzyme Commision number 3.1.8.1: aryldialkylphosphatase.
3.4.13.9: Xaa-Pro dipeptidase.
3.8.2.2: diisopropyl-fluorophosphatase.
Gene Ontology
Molecular Function
GO:0004063 aryldialkylphosphatase activity
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:0047862 diisopropyl-fluorophosphatase activity
GO:0102009 proline dipeptidase activity
Biological Process
GO:0006508 proteolysis
GO:0009636 response to toxic substance
Cellular Component
GO:0005829 cytosol

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:3l24, PDBe:3l24, PDBj:3l24
PDBsum3l24
PubMed20000741
UniProtQ44238|PEPQ_ALTSX Xaa-Pro dipeptidase (Gene Name=pepQ)

[Back to BioLiP]