Structure of PDB 3l24 Chain B Binding Site BS01
Receptor Information
>3l24 Chain B (length=417) Species:
232
(Alteromonas sp.) [
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MNKLAVLYAEHIATLQKRTREIIERENLDGVVFHSGQAKRQFLDDMYYPF
KVNPQFKAWLPVIDNPHCWIVANGTDKPKLIFYRPVDFWHKVPDEPNEYW
ADYFDIELLVKPDQVEKLLPYDKARFAYIGEYLEVAQALGFELMNPEPVM
NFYHYHRAYKTQYELACMREANKIAVQGHKAARDAFFQGKSEFEIQQAYL
LATQHSENDNPYGNIVALNENCAILHYTHFDRVAPATHRSFLIDAGANFN
GYAADITRTYDFTGEGEFAELVATMKQHQIALMNQLAPGKLYGELHLDCH
QRVAQTLSDFNIVDLSADEIVAKGITSTFFPHGLGHHIGLQVHDVTRKIE
ANQVFTIEPGLYFIDSLLGDLAATDNNQHINWDKVAELKPFGGIRIEDNI
IVHEDSLENMTRELRLR
Ligand information
Ligand ID
MN
InChI
InChI=1S/Mn/q+2
InChIKey
WAEMQWOKJMHJLA-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mn+2]
CACTVS 3.341
[Mn++]
Formula
Mn
Name
MANGANESE (II) ION
ChEMBL
DrugBank
DB06757
ZINC
PDB chain
3l24 Chain B Residue 518 [
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Receptor-Ligand Complex Structure
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PDB
3l24
Structural insights into the dual activities of the nerve agent degrading organophosphate anhydrolase/prolidase.
Resolution
2.3 Å
Binding residue
(original residue number in PDB)
D255 H336 T379 E381 E420
Binding residue
(residue number reindexed from 1)
D255 H336 T356 E358 E397
Annotation score
1
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
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Biological Process
View graph for
Cellular Component
External links
PDB
RCSB:3l24
,
PDBe:3l24
,
PDBj:3l24
PDBsum
3l24
PubMed
20000741
UniProt
Q44238
|PEPQ_ALTSX Xaa-Pro dipeptidase (Gene Name=pepQ)
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