Structure of PDB 1p6c Chain B

Receptor sequence
>1p6cB (length=330) Species: 239 (Flavobacterium sp.) [Search protein sequence]
DRINTVRGPITISEAGFTLTHEHICGSSAGFLRAWPEFFGSRKALAEKAV
RGLRRARAAGVRTIVDVSTFDIGRDVSLLAEVSRAADVHIVAATGLWFDP
PLSMRLRSVEELTQFFLREIQYGIEDTGIRAGIIKVATTGKATPFQELVL
KAAARASLATGVPVTTHTAASQRDGEQQAAIFESEGLSPSRVCIGHSDDT
DDLSYLTALAARGYLIGLDGIPWSAIGLEDNASASALLGIRSWQTRALLI
KALIDQGYMKQILVSNDWTFGFSSYVTNIMDVMDRVNPDGMAFIPLRVIP
FLREKGVPQETLAGITVTNPARFLSPTLRA
3D structure
PDB1p6c Enhanced degradation of chemical warfare agents through molecular engineering of the phosphotriesterase active site.
ChainB
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 K169 D301 H21 H23 K135 D267
BS02 ZN B K169 H201 H230 K135 H167 H196
BS03 EBP B Q155 Y156 Q121 Y122
BS04 DII B W131 H201 W97 H167
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1p6c, PDBe:1p6c, PDBj:1p6c
PDBsum1p6c
PubMed15369336
UniProtP0A433|OPD_SPHSA Parathion hydrolase (Gene Name=opd)

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