Structure of PDB 3ur5 Chain B

Receptor sequence

>3ur5B (length=323) Species: 293 (Brevundimonas diminuta)

DRINTVRGPITISEAGFTLTHEHICGSSAGFLRAWPEFFGSRKALAEKAV
RGLRRARAAGVRTIVDVSTFDIGRDVSLLAEVSRAADVHIVAATGLWFDP
PLSMRLRSVEELTQFFLREIQYGIEDTGIRAGIIKVATTGKATPFQELVL
RAAARASLATGVPVTTHTAASQRDGEQQAAIFESEGLSPSRVCIGHSDDT
DDLSYLTALAARGYLIGLDHIPHSAIGASASALLGNRSWQTRALLIKALI
DQGYMKQILVSNDWLFGFSSYVTNIMDVMDRVNPDGMAFIPLRVIPFLRE
KGVPQETLAGITVTNPARFLSPT

3D structure

• PDB: 3ur5 Enzymes for the homeland defense: optimizing phosphotriesterase for the hydrolysis of organophosphate nerve agents.
• Chain: B
• Resolution: 1.6 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H55 H57 K169 H201 H230 D233 H254 D301
• Catalytic site (residue number reindexed from 1): H21 H23 K135 H167 H196 D199 H220 D263
• Enzyme Commision number: 3.1.8.1: aryldialkylphosphatase.

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	DPF	B	W131 K169 H201 H230 H254 D301	W97 K135 H167 H196 H220 D263
BS02	CO	B	H55 H57 K169 D301	H21 H23 K135 D263
BS03	CO	B	K169 H201 H230	K135 H167 H196
BS04	CO	B	D233 H254	D199 H220

Gene Ontology

Molecular Function

• GO:0004063 aryldialkylphosphatase activity
• GO:0008270 zinc ion binding
• GO:0016787 hydrolase activity
• GO:0016788 hydrolase activity, acting on ester bonds
• GO:0046872 metal ion binding

Biological Process

• GO:0009056 catabolic process

Cellular Component

• GO:0005886 plasma membrane

External links

• PDB: RCSB:3ur5, PDBe:3ur5, PDBj:3ur5
• PDBsum: 3ur5
• PubMed: 22809162
• UniProt: P0A434|OPD_BREDI Parathion hydrolase (Gene Name=opd)