Structure of PDB 2r1l Chain A

Receptor sequence
>2r1lA (length=329) Species: 358 (Agrobacterium tumefaciens) [Search protein sequence]
TGDLINTVRGPIPVSEAGFTLTHEHICGSSAGFLRAWPEFFGSRKALAEK
AVRGLRHARAAGVQTIVDVSTFDIGRDVRLLAEVSRAADVHIVAATGLWF
DPPLSMRMRSVEELTQFFLREIQHGIEDTGIRAGIIKVATTGKATPFQEL
VLKAAARASLATGVPVTTHTSASQRDGEQQAAIFESEGLSPSRVCIGHSD
DTDDLSYLTGLAARGYLVGLDRMPYSAIGLEGDASALALFGTRSWQTRAL
LIKALIDRGYKDRILVSHDWLFGFSSYVTNIMDVMDRINPDGMAFVPLRV
IPFLREKGVPPETLAGVTVANPARFLSPT
3D structure
PDB2r1l In crystallo capture of a Michaelis complex and product-binding modes of a bacterial phosphotriesterase
ChainA
Resolution1.95 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 FE2 A H55 H57 K169 D301 H23 H25 K137 D269
BS02 CO A K169 H201 H230 K137 H169 H198
BS03 DPJ A W131 K169 H201 H230 R254 Y257 D301 F306 W99 K137 H169 H198 R222 Y225 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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:2r1l, PDBe:2r1l, PDBj:2r1l
PDBsum2r1l
PubMed18082180
UniProtQ93LD7

[Back to BioLiP]