Structure of PDB 3a3w Chain A

Receptor sequence
>3a3wA (length=329) Species: 358 (Agrobacterium tumefaciens) [Search protein sequence]
TGDLINTVRGPIPVSEAGFTLTHEHICASSAGFLRAWPEFFGSRKALVEK
AVRGLRHARAAGVQTIVDVSTFDIGRDVRLLAEVSQAADVHIVAATGLWF
DPPLSMRMRSVEELTQFFLREIQHGIEDTGIRAGIIKVATTGKATPFQEL
VLRAAARASLATGVPVTTHTSASPRGGEQQAAIFESEGLSPSRVCIGHSD
DTDDLSYLTGLAARGYLVGLDRMPYSATGLEGNASALALFSTRSWQTRAL
LIKALIDRGYKDRILVSHDWLFGFSSYVTNIMDVMDRINPDGMAFVPLRV
IPFLREKGVPPETLAGVTVANPARFLSPT
3D structure
PDB3a3w Conformational sampling, catalysis, and evolution of the bacterial phosphotriesterase
ChainA
Resolution1.85 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) H23 H25 K137 H169 H198 D201 R222 D269
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 H55 H57 K169 D301 H23 H25 K137 D269
BS02 CO A K169 H201 H230 K137 H169 H198
BS03 EPL A H57 W131 Y257 F306 S308 H25 W99 Y225 F274 S276
Gene Ontology
Molecular Function
GO:0008270 zinc ion binding
GO:0016788 hydrolase activity, acting on ester bonds
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:3a3w, PDBe:3a3w, PDBj:3a3w
PDBsum3a3w
PubMed19966226
UniProtQ93LD7

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