Structure of PDB 3htw Chain A

Receptor sequence
>3htwA (length=322) Species: 1299 (Deinococcus radiodurans) [Search protein sequence]
TAQTVTGAVAAAQLGATLPHEHVIFGYPGYAGDVTLGPFDHAAALASCTE
TARALLARGIQTVVDATPNDCGRNPAFLREVSEATGLQILCATGFYYEGE
GATTYFKFRASLGDAESEIYEMMRTEVTEGIAGTGIRAGVIKLASSRDAI
TPYEQLFFRAAARVQRETGVPIITHTQEGQQGPQQAELLTSLGADPARIM
IGHMDGNTDPAYHRETLRHGVSIAFDRIGLQGMVGTPTDAERLSVLTTLL
GEGYADRLLLSHDSIWHWLGRPPAIPEAALPAVKDWHPLHISDDILPDLR
RRGITEEQVGQMTVGNPARLFG
3D structure
PDB3htw Structure-based and random mutagenesis approaches increase the organophosphate-degrading activity of a phosphotriesterase homologue from Deinococcus radiodurans.
ChainA
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H121 H123 K243 H276 H304 G307 R328 D364
Catalytic site (residue number reindexed from 1) H20 H22 K142 H175 H203 G206 R227 D263
Enzyme Commision number ?
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 H121 H123 K243 D364 H20 H22 K142 D263
BS02 CO A K243 H276 H304 K142 H175 H203
BS03 MG A R402 R403 R301 R302
Gene Ontology
Molecular Function
GO:0008270 zinc ion binding
GO:0016788 hydrolase activity, acting on ester bonds
GO:0046573 lactonohydrolase activity
GO:0046872 metal ion binding
Biological Process
GO:0009056 catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3htw, PDBe:3htw, PDBj:3htw
PDBsum3htw
PubMed19631223
UniProtQ9RVU2

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