Structure of PDB 2d2g Chain A

Receptor sequence
>2d2gA (length=329) Species: 358 (Agrobacterium tumefaciens) [Search protein sequence]
TGDLINTVRGPIPVSEAGFTLTHEHICGSSAGFLRAWPEFFGSRKALAEK
AVRGLRHARAAGVQTIVDVSTFDIGRDVRLLAEVSRAADVHIVAATGLWF
DPPLSMRMRSVEELTQFFLREIQHGIEDTGIRAGIIKVATTGKATPFQEL
VLKAAARASLATGVPVTTHTSASQRDGEQQAAIFESEGLSPSRVCIGHSD
DTDDLSYLTGLAARGYLVGLDRMPYSAIGLEGNASALALFGTRSWQTRAL
LIKALIDRGYKDRILVSHDWLFGFSSYVTNIMDVMDRINPDGMAFVPLRV
IPFLREKGVPPETLAGVTVANPARFLSPT
3D structure
PDB2d2g The structure of an enzyme-product complex reveals the critical role of a terminal hydroxide nucleophile in the bacterial phosphotriesterase mechanism
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 DZZ A H57 W131 K169 H201 R254 D301 F306 H25 W99 K137 H169 R222 D269 F274
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:2d2g, PDBe:2d2g, PDBj:2d2g
PDBsum2d2g
PubMed16054447
UniProtQ93LD7

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