Structure of PDB 1psc Chain A

Receptor sequence
>1pscA (length=329) Species: 293 (Brevundimonas diminuta) [Search protein sequence]
DRINTVRGPITISEAGFTLTHEHICGSSAGFLRAWPEFFGSRKALAEKAV
RGLRRARAAGVRTIVDVSTFDIGRDVSLLAEVSRAADVHIVAATGLWFDP
PLSMRLRSVEELTQFFLREIQYGIEDTGIRAGIIKVATTGKATPFQELVL
KAAARASLATGVPVTTHTAASQRDGEQQAAIFESEGLSPSRVCIGHSDDT
DDLSYLTALAARGYLIGLDHIPHSAIGLEDNASASALLGIRSWQTRALLI
KALIDQGYMKQILVSNDWLFGFSSYVTNIMDVMDRVNPDGMAFIPLRVIP
FLREKGVPQETLAGITVTNPARFLSPTLR
3D structure
PDB1psc Three-dimensional structure of the binuclear metal center of phosphotriesterase.
ChainA
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 H254 D301
Catalytic site (residue number reindexed from 1) H21 H23 K135 H167 H196 D199 H220 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 CD A H55 H57 D301 H21 H23 D267
BS02 CD A H201 H230 H167 H196
Gene Ontology
Molecular Function
GO:0008270 zinc ion binding
GO:0016788 hydrolase activity, acting on ester bonds
Biological Process
GO:0009056 catabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1psc, PDBe:1psc, PDBj:1psc
PDBsum1psc
PubMed7794910
UniProtP0A434|OPD_BREDI Parathion hydrolase (Gene Name=opd)

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