Structure of PDB 5j23 Chain D Binding Site BS01

Receptor Information
>5j23 Chain D (length=318) Species: 266834 (Sinorhizobium meliloti 1021) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
RPRILVPGKINPRVLERLPEMFETVRIERADAALVTADMRDVSGIAVSGK
LPVPLMDAFPSLEIVANFGVGYDGVDVSRAAARGIVVTNTPDVLTEEVAD
TAIGLLLNTLRLLPQAEQWLRQGRWVREGAFPLSPLSLRGRTVGLFGLGR
IGLAIARRLEAFGVSIAYHTRTPREGLGFTYHPTLVGMAEAVDTLIVIVP
GTASTLKAVNADVLSALGPKGVLINVGRGSTVDEAALVTALQNGTIAGAG
LDVFENEPNVPEALLSFPNVSLLPHVASASVVTRNAMSDLVVDNLKAWFS
TGEALTPVAETPFRRRAI
Ligand information
Ligand IDA2R
InChIInChI=1S/C15H24N5O17P3/c16-12-7-13(18-3-17-12)20(4-19-7)14-11(36-38(25,26)27)9(22)6(34-14)2-33-40(30,31)37-39(28,29)32-1-5-8(21)10(23)15(24)35-5/h3-6,8-11,14-15,21-24H,1-2H2,(H,28,29)(H,30,31)(H2,16,17,18)(H2,25,26,27)/t5-,6-,8-,9-,10-,11-,14-,15-/m1/s1
InChIKeyICNHOLCERMYLRZ-KEOHHSTQSA-N
SMILES
SoftwareSMILES
CACTVS 3.341Nc1ncnc2n(cnc12)[CH]3O[CH](CO[P](O)(=O)O[P](O)(=O)OC[CH]4O[CH](O)[CH](O)[CH]4O)[CH](O)[CH]3O[P](O)(O)=O
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@](=O)(O)O[P@@](=O)(O)OC[C@@H]4[C@H]([C@H]([C@@H](O4)O)O)O)O)OP(=O)(O)O)N
ACDLabs 10.04O=P(O)(O)OC3C(O)C(OC3n1c2ncnc(N)c2nc1)COP(=O)(O)OP(=O)(O)OCC4OC(O)C(O)C4O
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)OP(=O)(O)OCC4C(C(C(O4)O)O)O)O)OP(=O)(O)O)N
CACTVS 3.341Nc1ncnc2n(cnc12)[C@@H]3O[C@H](CO[P@@](O)(=O)O[P@](O)(=O)OC[C@H]4O[C@@H](O)[C@H](O)[C@@H]4O)[C@@H](O)[C@H]3O[P](O)(O)=O
FormulaC15 H24 N5 O17 P3
Name[(2R,3R,4R,5R)-5-(6-AMINO-9H-PURIN-9-YL)-3-HYDROXY-4-(PHOSPHONOOXY)TETRAHYDROFURAN-2-YL]METHYL [(2R,3S,4R,5R)-3,4,5-TRIHYDROXYTETRAHYDROFURAN-2-YL]METHYL DIHYDROGEN DIPHOSPHATE
ChEMBL
DrugBank
ZINCZINC000044460250
PDB chain5j23 Chain D Residue 403 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB5j23 Structural, Biochemical, and Evolutionary Characterizations of Glyoxylate/Hydroxypyruvate Reductases Show Their Division into Two Distinct Subfamilies.
Resolution2.3 Å
Binding residue
(original residue number in PDB)		V72 F148 L150 G151 R152 I153 T172 R173 V201 P202 S206 T207 G229 R230
Binding residue
(residue number reindexed from 1)		V70 F146 L148 G149 R150 I151 T170 R171 V199 P200 S204 T205 G227 R228
Annotation score3
Enzymatic activity
Catalytic site (original residue number in PDB) L96 R230 D254 E259 H277
Catalytic site (residue number reindexed from 1) L94 R228 D252 E257 H275
Enzyme Commision number ?
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0016491 oxidoreductase activity
GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
GO:0016618 hydroxypyruvate reductase [NAD(P)H] activity
GO:0030267 glyoxylate reductase (NADPH) activity
GO:0046872 metal ion binding
GO:0051287 NAD binding
Cellular Component
GO:0005829 cytosol

View graph for
Molecular Function
View graph for
Cellular Component
External links
PDB RCSB:5j23, PDBe:5j23, PDBj:5j23
PDBsum5j23
PubMed29309127
UniProtQ92LZ4

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