Structure of PDB 1p6b Chain B

Receptor sequence

>1p6bB (length=331) Species: 239 (Flavobacterium sp.)

GDRINTVRGPITISEAGFTLTHEHICGSSAGFLRAWPEFFGSRKALAEKA
VRGLRRARAAGVRTIVDVSTFDIGRDVSLLAEVSRAADVHIVAATGLWFD
PPLSMRLRSVEELTQFFLREIQYGIEDTGIRAGIIKVATTGKATPFQELV
LKAAARASLATGVPVTTHTAASQRDGEQQAAIFESEGLSPSRVCIGHSDD
TDDLSYLTALAARGYLIGLDGIPWSAIGLEDNASASALLGIRSWQTRALL
IKALIDQGYMKQILVSNDWTFGFSSYVTNIMDVMDRVNPDGMAFIPLRVI
PFLREKGVPQETLAGITVTNPARFLSPTLRA

3D structure

• PDB: 1p6b Enhanced degradation of chemical warfare agents through molecular engineering of the phosphotriesterase active site.
• Chain: B
• Resolution: 1.9 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): H22 H24 K136 H168 H197 D200 G221 D268
• 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 K169 D301	H22 H24 K136 D268
BS02	ZN	B	K169 H201 H230	K136 H168 H197
BS03	ZN	B	H230 D253	H197 D220
BS04	EBP	B	Q155 Y156	Q122 Y123
BS05	EFS	B	F132 T173	F99 T140

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:1p6b, PDBe:1p6b, PDBj:1p6b
• PDBsum: 1p6b
• PubMed: 15369336
• UniProt: P0A433|OPD_SPHSA Parathion hydrolase (Gene Name=opd)