Structure of PDB 1eq2 Chain B Binding Site BS02

Receptor Information
>1eq2 Chain B (length=300) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MIIVTGGAGFIGSNIVKALNDKGITDILVVDNLKDGTKFVNLVDLNIADY
MDKEDFLIQIMAGEEFGDVEAIFHEGACSSTTEWDGKYMMDNNYQYSKEL
LHYCLEREIPFLYASSAATYGGRTSDFIESREYEKPLNVYGYSKFLFDEY
VRQILPEANSQIVGFRYFNVYGPREGHKGSMASVAFHLNTQLNNGESPKL
FEGSENFKRDFVYVGDVADVNLWFLENGVSGIFNLGTGRAESFQAVADAT
LAYHKKGQIEYIPFYQAFTQADLTNLRAAGYDKPFKTVAEGVTEYMAWLN
Ligand information
Ligand IDADQ
InChIInChI=1S/C16H25N5O15P2/c17-13-7-14(19-3-18-13)21(4-20-7)15-11(26)9(24)6(33-15)2-32-37(28,29)36-38(30,31)35-16-12(27)10(25)8(23)5(1-22)34-16/h3-6,8-12,15-16,22-27H,1-2H2,(H,28,29)(H,30,31)(H2,17,18,19)/t5-,6-,8-,9-,10+,11-,12-,15-,16-/m1/s1
InChIKeyWFPZSXYXPSUOPY-ROYWQJLOSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)OP(=O)(O)OC4C(C(C(C(O4)CO)O)O)O)O)O)N
CACTVS 3.341Nc1ncnc2n(cnc12)[C@@H]3O[C@H](CO[P@](O)(=O)O[P@](O)(=O)O[C@H]4O[C@H](CO)[C@@H](O)[C@H](O)[C@H]4O)[C@@H](O)[C@H]3O
ACDLabs 10.04O=P(OC1OC(C(O)C(O)C1O)CO)(O)OP(=O)(O)OCC4OC(n2c3ncnc(N)c3nc2)C(O)C4O
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)O[C@@H]4[C@@H]([C@H]([C@@H]([C@H](O4)CO)O)O)O)O)O)N
CACTVS 3.341Nc1ncnc2n(cnc12)[CH]3O[CH](CO[P](O)(=O)O[P](O)(=O)O[CH]4O[CH](CO)[CH](O)[CH](O)[CH]4O)[CH](O)[CH]3O
FormulaC16 H25 N5 O15 P2
NameADENOSINE-5'-DIPHOSPHATE-GLUCOSE;
ADENOSINE-5'-MONOPHOSPHATE GLUCOPYRANOSYL-MONOPHOSPHATE ESTER
ChEMBLCHEMBL227552
DrugBankDB01774
ZINCZINC000008216005
PDB chain1eq2 Chain B Residue 2501 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1eq2 The crystal structure of ADP-L-glycero-D-mannoheptose 6-epimerase: catalysis with a twist.
Resolution2.0 Å
Binding residue
(original residue number in PDB)		F168 N169 S180 H187 L200 F201 R209 F243 Y272 Q273
Binding residue
(residue number reindexed from 1)		F168 N169 S180 H187 L200 F201 R209 F243 Y265 Q266
Annotation score3
Enzymatic activity
Catalytic site (original residue number in PDB) S116 Y140 K144 K178
Catalytic site (residue number reindexed from 1) S116 Y140 K144 K178
Enzyme Commision number 5.1.3.20: ADP-glyceromanno-heptose 6-epimerase.
Gene Ontology
Molecular Function
GO:0005515 protein binding
GO:0008712 ADP-glyceromanno-heptose 6-epimerase activity
GO:0016853 isomerase activity
GO:0050661 NADP binding
GO:0070401 NADP+ binding
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0009103 lipopolysaccharide biosynthetic process
GO:0009244 lipopolysaccharide core region biosynthetic process
GO:0097171 ADP-L-glycero-beta-D-manno-heptose biosynthetic process
Cellular Component
GO:0005829 cytosol
GO:0016020 membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1eq2, PDBe:1eq2, PDBj:1eq2
PDBsum1eq2
PubMed10896473
UniProtP67910|HLDD_ECOLI ADP-L-glycero-D-manno-heptose-6-epimerase (Gene Name=hldD)

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