Structure of PDB 4zwp Chain B

Receptor sequence
>4zwpB (length=428) Species: 232 (Alteromonas sp.) [Search protein sequence]
NKLAVLYAEHIATLQKRTREIIERENLDGVVFHSGQAKRQFLDDMYYPFK
VNPQFKAWLPVIDNPHCWIVANGTDKPKLIFYRPVDFWHPNEYWADYFDI
ELLVKPDQVEKLLPYDKARFAYIGEYLEVAQALGFELMNPEPVMNFYHYH
RAYKTQYELACMREANKIAVQGHKAARDAFFQGKSEFEIQQAYLLATQHS
ENDTPFGNIVALNENCAILHYTHFDRVAPATHRSFLIDAGANFNGYAADI
TRTYDFTGEGEFAELVATMKQHQIALCNQLAPGKLYGELHLDCHQRVAQT
LSDFNIVNLSADEIVAKGITSTFFPHGLGHHIGLQVHDVGGFMADEQGAH
QEPPRCTRKIEANQVFTIEPGLYFIDSLLGDLAATDNNQHINWDKVAELK
PFGGIRIEDNIIVHEDSLENMTRELELD
3D structure
PDB4zwp Engineering the Organophosphorus Acid Anhydrolase Enzyme for Increased Catalytic Efficiency and Broadened Stereospecificity on Russian VX.
ChainB
Resolution2.397 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) D44 H220 D238 D249 H326 H330 H337 E369 Y373 R406 E408
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 MN B D244 D255 E420 D238 D249 E408
BS02 MN B D255 H336 E381 E420 D249 H330 E369 E408
BS03 M44 B F212 D244 D255 H332 H343 E381 E420 F206 D238 D249 H326 H337 E369 E408
Gene Ontology
Molecular Function
GO:0016795 phosphoric triester hydrolase activity

View graph for
Molecular Function
External links
PDB RCSB:4zwp, PDBe:4zwp, PDBj:4zwp
PDBsum4zwp
PubMed26418828
UniProtQ44238|PEPQ_ALTSX Xaa-Pro dipeptidase (Gene Name=pepQ)

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