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Receptor Information

>1khz Chain A (length=205) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

MLKPDNLPVTFGKNDVEIIARETLYRGFFSLDLYRFRHRLFNGQMSHEVR
REIFERGHAAVLLPFDPVRDEVVLIEQIRIAAYDTSETPWLLEMVAGMIE
EGESVEDVARREAIEEAGLIVKRTKPVLSFLASPGGTSERSSIMVGEVDA
TTASLADENEDIRVHVVSREQAYQWVEEGKIDNAASVIALQWLQLHHQAL
KNEWA

Ligand ID

ADV

InChI

InChI=1S/C16H25N5O13P2/c17-13-8-14(19-3-18-13)21(4-20-8)15-11(24)9(22)6(33-15)1-31-35(27,28)5-36(29,30)32-2-7-10(23)12(25)16(26)34-7/h3-4,6-7,9-12,15-16,22-26H,1-2,5H2,(H,27,28)(H,29,30)(H2,17,18,19)/t6-,7-,9-,10-,11-,12-,15-,16+/m1/s1

InChIKey

ZPZRETFSCSWNDT-DBXCYWGHSA-N

SMILES

Software	SMILES
CACTVS 3.341	Nc1ncnc2n(cnc12)[CH]3O[CH](CO[P](O)(=O)C[P](O)(=O)OC[CH]4O[CH](O)[CH](O)[CH]4O)[CH](O)[CH]3O
OpenEye OEToolkits 1.5.0	c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(CP(=O)(O)OCC4C(C(C(O4)O)O)O)O)O)O)N
OpenEye OEToolkits 1.5.0	c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@@](=O)(C[P@](=O)(O)OC[C@@H]4[C@H]([C@H]([C@H](O4)O)O)O)O)O)O)N
CACTVS 3.341	Nc1ncnc2n(cnc12)[C@@H]3O[C@H](CO[P@@](O)(=O)C[P@@](O)(=O)OC[C@H]4O[C@H](O)[C@H](O)[C@@H]4O)[C@@H](O)[C@H]3O
ACDLabs 10.04	O=P(O)(OCC3OC(n1c2ncnc(N)c2nc1)C(O)C3O)CP(=O)(O)OCC4OC(O)C(O)C4O

Formula

C16 H25 N5 O13 P2

Name

ALPHA-BETA METHYLENE ADP-RIBOSE;
AMPCPR;
{[5-(6-AMINO-PURIN-9-YL)-3,4-DIHYDROXY-TETRAHYDRO-FURAN-2-YLMETHOXY]-HYDROXY-PHOSPHORYLMETHYL}-PHOSPHONIC ACID MONO-(3,4,5-TRIHYDROXY-TETRAHYDRO-FURAN-2-YLMETHYL) ESTER

PDB chain

1khz Chain B Residue 402 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

Receptor-Ligand Complex Structure

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Structure summary

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PDB	1khz Mechanism of the Escherichia coli ADP-ribose pyrophosphatase, a Nudix hydrolase.
Resolution	2.04 Å
Binding residue (original residue number in PDB)	R51 E52 S133 G135
Binding residue (residue number reindexed from 1)	R51 E52 S133 G135
Annotation score	3

Enzyme Commision number

3.6.1.13: ADP-ribose diphosphatase.

	Molecular Function
GO:0000287	magnesium ion binding
GO:0005515	protein binding
GO:0016462	pyrophosphatase activity
GO:0016787	hydrolase activity
GO:0016818	hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
GO:0019144	ADP-sugar diphosphatase activity
GO:0042803	protein homodimerization activity
GO:0046872	metal ion binding
GO:0047631	ADP-ribose diphosphatase activity

	Biological Process
GO:0006753	nucleoside phosphate metabolic process
GO:0009408	response to heat
GO:0019693	ribose phosphate metabolic process

	Cellular Component
GO:0005829	cytosol

PDB	RCSB:1khz, PDBe:1khz, PDBj:1khz
PDBsum	1khz
PubMed	12135348
UniProt	Q93K97\|ADPP_ECOLI ADP-ribose pyrophosphatase (Gene Name=nudF)

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Structure of PDB 1khz Chain A Binding Site BS01