Structure of PDB 3e3h Chain A

Receptor sequence
>3e3hA (length=336) Species: 293 (Brevundimonas diminuta) [Search protein sequence]
SIGTGDRINTVRGPITISEAGFTLTHEHICGSSAGFLRAWPEFFGSRKAL
AEKAVRGLRRARAAGVRTIVDVSTFDIGRDVSLLAEVSRAADVHIVAATG
LWFDPPLSMRLRSVEELTQFFLREIQYGIEDTGIRAGIIKVATTGKATPF
QELVLKAAARASLATGVPVTTHTAASQRDGEQQAAIFESEGLSPSRVCIG
HSDDTDDLSYLTALAARGYLIGLDRIPFSAIGLEDNASASALLGIRSWQT
RALLIKALIDQGYMKQILVSNDWLFGFSSYVTNIMDVMDRVNPDGMAFIP
LRVIPFLREKGVPQETLAGITVTNPARFLSPTLRAS
3D structure
PDB3e3h Balancing the stability and the catalytic specificities of OP hydrolases with enhanced V-agent activities.
ChainA
Resolution2.15 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 R254 D301
Catalytic site (residue number reindexed from 1) H26 H28 K140 H172 H201 D204 R225 D272
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 CO A K169 H201 H230 K140 H172 H201
BS02 CO A H55 H57 K169 D301 H26 H28 K140 D272
BS03 EBP A F51 R96 F22 R67
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:3e3h, PDBe:3e3h, PDBj:3e3h
PDBsum3e3h
PubMed18434422
UniProtP0A434|OPD_BREDI Parathion hydrolase (Gene Name=opd)

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