Structure of PDB 4zwo Chain A

Receptor sequence
>4zwoA (length=425) Species: 232 (Alteromonas sp.) [Search protein sequence]
NKLAVLYAEHIATLQKRTREIIERENLDGVVFHSGQAKRQFLDDMYYPFK
VNPQFKAWLPVIDNPHCWIVANGTDKPKLIFYRPVDFWHKNEYWADYFDI
ELLVKPDQVEKLLPYDKARFAYIGEYLEVAQALGFELMNPEPVMNFYHYH
RAYKTQYELACMREANKIAVQGHKAARDAFFQGKSEFEIQQAYLLATQHS
ENDTPFGNIVALNENCAILHYTHFDRVAPATHRSFLIDAGANFNGYAADI
TRTYDFTGEGEFAELVATMKQHQIALCNQLAPGKLYGELHLDCHQRVAQT
LSDFNIVNLSADEIVAKGITSTFFPHGLGHHIGLQVHDVGGFMADEQGAF
LRCTRKIEANQVFTIEPGLYFIDSLLGDLAATDNNQHINWDKVAELKPFG
GIRIEDNIIVHEDSLENMTRELELD
3D structure
PDB4zwo Engineering the Organophosphorus Acid Anhydrolase Enzyme for Increased Catalytic Efficiency and Broadened Stereospecificity on Russian VX.
ChainA
Resolution2.141 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 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 MN A D255 H336 E381 E420 D249 H330 E366 E405
BS02 MN A D244 D255 E420 D238 D249 E405
BS03 MN A R25 N27 R24 N26
BS04 MN A E24 N27 E23 N26
BS05 GOA A F212 D244 D255 H343 F206 D238 D249 H337
Gene Ontology
Molecular Function
GO:0016795 phosphoric triester hydrolase activity

View graph for
Molecular Function
External links
PDB RCSB:4zwo, PDBe:4zwo, PDBj:4zwo
PDBsum4zwo
PubMed26418828
UniProtQ44238|PEPQ_ALTSX Xaa-Pro dipeptidase (Gene Name=pepQ)

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