Structure of PDB 4zwp Chain A

Receptor sequence
>4zwpA (length=422) Species: 232 (Alteromonas sp.) [Search protein sequence]
KLAVLYAEHIATLQKRTREIIERENLDGVVFHSGQAKRQFLDDMYYPFKV
NPQFKAWLPVIDNPHCWIVANGTDKPKLIFYRPVDFWNEYWADYFDIELL
VKPDQVEKLLPYDKARFAYIGEYLEVAQALGFELMNPEPVMNFYHYHRAY
KTQYELACMREANKIAVQGHKAARDAFFQGKSEFEIQQAYLLATQHSEND
TPFGNIVALNENCAILHYTHFDRVAPATHRSFLIDAGANFNGYAADITRT
YDFTGEGEFAELVATMKQHQIALCNQLAPGKLYGELHLDCHQRVAQTLSD
FNIVNLSADEIVAKGITSTFFPHGLGHHIGLQVHDVGGFMADEQGAFLRC
TRKIEANQVFTIEPGLYFIDSLLGDLAATDNNQHINWDKVAELKPFGGIR
IEDNIIVHEDSLENMTRELELD
3D structure
PDB4zwp Engineering the Organophosphorus Acid Anhydrolase Enzyme for Increased Catalytic Efficiency and Broadened Stereospecificity on Russian VX.
ChainA
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) D43 H217 D235 D246 H323 H327 H334 E363 Y367 R400 E402
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 T379 E381 E420 D246 H327 T361 E363 E402
BS02 MN A D244 D255 E420 D235 D246 E402
BS03 MN A L28 D29 L26 D27
BS04 M44 A F212 D244 D255 H332 H343 E381 F203 D235 D246 H323 H334 E363
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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