Structure of PDB 6gbj Chain A

Receptor sequence
>6gbjA (length=331) Species: 293 (Brevundimonas diminuta) [Search protein sequence]
DRINTVRGPITISEAGFTLMHEHICGSSAGFLRAWPEFFGSRDALAEKAV
RGLRRARAAGVRTIVDVSTFDIGRDVELLAEVSEAADVHIVAATGLWFDP
PLSMRLRSVEELTQFFLREIQYGIEDTGIRAGIIKVATTGKATPFQERVL
RAAARASLATGVPVTTHTDASQRDGEQQADIFESEGLDPSRVCIGHSDDT
DDLDYLTALAARGYLIGLDRIPWSAIGLEDNASAAALLGLRSWQTRALLI
KALIDQGYADQILVSNDWTFGFSSYVTNIMDVLDRVNPDGMAFIPLRVIP
FLREKGVPDETLETIMVDNPARFLSPTLRAS
3D structure
PDB6gbj Automated Design of Efficient and Functionally Diverse Enzyme Repertoires.
ChainA
Resolution1.63 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) H21 H23 K135 H167 H196 D199 R220 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 A H55 H57 D301 H21 H23 D267
BS02 ZN A H201 H230 H167 H196
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:6gbj, PDBe:6gbj, PDBj:6gbj
PDBsum6gbj
PubMed30270109
UniProtP0A434|OPD_BREDI Parathion hydrolase (Gene Name=opd)

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