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BioLiP

Structure of PDB 2r1p Chain A

Receptor sequence
>2r1pA (length=328) Species: 358 (Agrobacterium tumefaciens) [Search protein sequence]
GDLINTVRGPIPVSEAGFTLTHEHICGSSAGFLRAWPEFFGSRKALAEKA
VRGLRHARAAGVQTIVDVSTFDIGRDVRLLAEVSRAADVHIVAATGLWFD
PPLSMRMRSVEELTQFFLREIQHGIEDTGIRAGIIKVATTGKATPFQELV
LRAAARASLATGVPVTTHTSASQRDGEQQAAIFESEGLSPSRVCIGHSDD
TDDLSYLTGLAARGYLVGLDRMPYSAIGLEGNASALALFGTRSWQTRALL
IKALIDRGYKDRILVSHDWLFGFSSYVTNIMDVMDRINPDGMAFVPLRVI
PFLREKGVPPETLAGVTVANPARFLSPT
3D structure
PDB2r1p In crystallo capture of a Michaelis complex and product-binding modes of a bacterial phosphotriesterase
ChainA
Resolution1.8 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) H22 H24 K136 H168 H197 D200 R221 D268
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 FE2 A H55 H57 K169 D301 H22 H24 K136 D268
BS02 CO A K169 H201 H230 K136 H168 H197
BS03 DPJ A W131 K169 H201 H230 R254 Y257 L271 D301 W98 K136 H168 H197 R221 Y224 L238 D268
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

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