Structure of PDB 3l7g Chain A

Receptor sequence
>3l7gA (length=425) Species: 232 (Alteromonas sp.) [Search protein sequence]
MNKLAVLYAEHIATLQKRTREIIERENLDGVVFHSGQAKRQFLDDMYYPF
KVNPQFKAWLPVIDNPHCWIVANGTDKPKLIFYRPVDFWHKVPDEPNEYW
ADYFDIELLVKPDQVEKLLPYDKARFAYIGEYLEVAQALGFELMNPEPVM
NFYHYHRAYKTQYELACMREANKIAVQGHKAARDAFFQGKSEFEIQQAYL
LATQHSENDNPYGNIVALNENCAILHYTHFDRVAPATHRSFLIDAGANFN
GYAADITRTYDFTGEGEFAELVATMKQHQIALMNQLAPGKLYGELHLDCH
QRVAQTLSDFNIVDLSADEIVAKGITSTFFPHGLGHHIGLQVHDVGGFMA
LRCTRKIEANQVFTIEPGLYFIDSLLGDLAATDNNQHINWDKVAELKPFG
GIRIEDNIIVHEDSLENMTRELRLR
3D structure
PDB3l7g Structural insights into the dual activities of the nerve agent degrading organophosphate anhydrolase/prolidase.
ChainA
Resolution2.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 E366 Y370 R403 E405
Enzyme Commision number 3.1.8.1: aryldialkylphosphatase.
3.4.13.9: Xaa-Pro dipeptidase.
3.8.2.2: diisopropyl-fluorophosphatase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 M44 A Y212 D244 D255 H332 H343 E381 R418 E420 Y212 D244 D255 H332 H343 E366 R403 E405 PDBbind-CN: -logKd/Ki=3.30,Ki=0.5mM
BS02 MN A D255 H336 T379 E381 E420 D255 H336 T364 E366 E405
BS03 MN A D244 D255 E420 D244 D255 E405
BS04 MN A D105 E107 D105 E107
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

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Molecular Function
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Cellular Component
External links
PDB RCSB:3l7g, PDBe:3l7g, PDBj:3l7g
PDBsum3l7g
PubMed20000741
UniProtQ44238|PEPQ_ALTSX Xaa-Pro dipeptidase (Gene Name=pepQ)

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