Structure of PDB 4zwu Chain B

Receptor sequence
>4zwuB (length=435) Species: 232 (Alteromonas sp.) [Search protein sequence]
NKLAVLYAEHIATLQKRTREIIERENLDGVVFHSGQAKRQFLDDMYYPFK
VNPQFKAWLPVIDNPHCWIVANGTDKPKLIFYRPVDFWHEPNEYWADYFD
IELLVKPDQVEKLLPYDKARFAYIGEYLEVAQALGFELMNPEPVMNFYHY
HRAYKTQYELACMREANKIAVQGHKAARDAFFQGKSEFEIQQAYLLATQH
SENDTPFGNYVALNENCAILHYTHFDRVAPATHRSFLIDAGANFNGYAAD
ITRTYDFTGEGEFAELVATMKQHQIALCNQLAPGKLYGELHLDCHQRVAQ
TLSDFNIVNLSADEIVAKGITSTFFPHGLGHHIGLQLHDVGGFMADEQGA
HQEPPEGHPFLRCTRKIEANQVFTIEPGLYFIDSLLGDLAATDNNQHINW
DKVAELKPFGGIRIEDNIIVHEDSLENMTRELELD
3D structure
PDB4zwu Engineering the Organophosphorus Acid Anhydrolase Enzyme for Increased Catalytic Efficiency and Broadened Stereospecificity on Russian VX.
ChainB
Resolution2.2 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 H221 D239 D250 H327 H331 H338 E376 Y380 R413 E415
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 GOA B F212 D255 H343 F207 D250 H338
BS02 MN B D244 D255 E420 D239 D250 E415
BS03 MN B D255 H336 E381 E420 D250 H331 E376 E415
Gene Ontology
Molecular Function
GO:0016795 phosphoric triester hydrolase activity

View graph for
Molecular Function
External links
PDB RCSB:4zwu, PDBe:4zwu, PDBj:4zwu
PDBsum4zwu
PubMed26418828
UniProtQ44238|PEPQ_ALTSX Xaa-Pro dipeptidase (Gene Name=pepQ)

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