Structure of PDB 6fs3 Chain B

Receptor sequence

>6fs3B (length=331) Species: 293 (Brevundimonas diminuta)

DRINTVRGPITISEAGFTLTHEHICGSSAGFLRAWPEFFGSRAALVEKAV
RGLRRARAAGVRTIVDVSTFDAGRDVSLLAEVSRAADVHIVAATGLWEDP
PLSMRLRSVEELTQFFLREIQYGIEDTGIRAGIIKVATQGKATPFQELVL
RAAARASLATGVPVTTHTFASQRDGEQQAAIFESEGLSPSRVCIGHSDDT
DDLSYLTALAARGYLIGLDGIPHSAIGLEDNASASALLGNRSWQTRALLI
KALIDQGYMKQILVSNDWLFGFSSYVTNIMDVMDSVNPDGMAFIPLRVIP
FLREKGVPQETLAGITVTNPARFLSPTLRAS

3D structure

• PDB: 6fs3 Crystal structures of Bacterail Phosphotriesterase variant with high catalytic activity towards organophosphate nerve agents developed by use of structure-based design and molecular evolution
• Chain: B
• Resolution: 1.75 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H55 H57 K169 H201 H230 D233 G254 D301
• Catalytic site (residue number reindexed from 1): H21 H23 K135 H167 H196 D199 G220 D267
• 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	ZN	B	H55 H57 D301	H21 H23 D267
BS02	ZN	B	H201 H230	H167 H196
BS03	9ON	B	H57 H201 H230 D301	H23 H167 H196 D267

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:6fs3, PDBe:6fs3, PDBj:6fs3
• PDBsum: 6fs3
• UniProt: P0A434|OPD_BREDI Parathion hydrolase (Gene Name=opd)