Structure of PDB 1e7s Chain A Binding Site BS01

Receptor Information
>1e7s Chain A (length=314) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KQRVFIAGHRGMVGSAIRRQLEQRGDVELVLRTRDELNLLDSRAVHDFFA
SERIDQVYLAAAKVGGIVANNTYPADFIYQNMMIESNIIHAAHQNDVNKL
LFLGSSCIYPKLAKQPMAESELLQGTLEPTNEPYAIARIAGIKLCESYNR
QYGRDYRSVMPTNLYGPHDNFHPSNSHVIPALLRRFHEATAQSAPDVVVW
GSGTPMREFLHVDDMAAASIHVMELAHEVWLENTQPMLSHINVGTGVDCT
IRELAQTIAKVVGYKGRVVFDASKPDGTPRKLLDVTRLHQLGWYHEISLE
AGLASTYQWFLENQ
Ligand information
Ligand IDNAP
InChIInChI=1S/C21H28N7O17P3/c22-17-12-19(25-7-24-17)28(8-26-12)21-16(44-46(33,34)35)14(30)11(43-21)6-41-48(38,39)45-47(36,37)40-5-10-13(29)15(31)20(42-10)27-3-1-2-9(4-27)18(23)32/h1-4,7-8,10-11,13-16,20-21,29-31H,5-6H2,(H7-,22,23,24,25,32,33,34,35,36,37,38,39)/t10-,11-,13-,14-,15-,16-,20-,21-/m1/s1
InChIKeyXJLXINKUBYWONI-NNYOXOHSSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1cc(c[n+](c1)C2C(C(C(O2)COP(=O)([O-])OP(=O)(O)OCC3C(C(C(O3)n4cnc5c4ncnc5N)OP(=O)(O)O)O)O)O)C(=O)N
CACTVS 3.341NC(=O)c1ccc[n+](c1)[CH]2O[CH](CO[P]([O-])(=O)O[P](O)(=O)OC[CH]3O[CH]([CH](O[P](O)(O)=O)[CH]3O)n4cnc5c(N)ncnc45)[CH](O)[CH]2O
CACTVS 3.341NC(=O)c1ccc[n+](c1)[C@@H]2O[C@H](CO[P]([O-])(=O)O[P@@](O)(=O)OC[C@H]3O[C@H]([C@H](O[P](O)(O)=O)[C@@H]3O)n4cnc5c(N)ncnc45)[C@@H](O)[C@H]2O
OpenEye OEToolkits 1.5.0c1cc(c[n+](c1)[C@H]2[C@@H]([C@@H]([C@H](O2)CO[P@@](=O)([O-])O[P@](=O)(O)OC[C@@H]3[C@H]([C@H]([C@@H](O3)n4cnc5c4ncnc5N)OP(=O)(O)O)O)O)O)C(=O)N
FormulaC21 H28 N7 O17 P3
NameNADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE;
2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE
ChEMBLCHEMBL295069
DrugBankDB03461
ZINC
PDB chain1e7s Chain A Residue 1317 [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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PDB1e7s Probing the Catalytic Mechanism of Gdp-4-Keto-6-Deoxy-D-Mannose Epimerase/Reductase by Kinetic and Crystallographic Characterization of Site-Specific Mutants
Resolution1.5 Å
Binding residue
(original residue number in PDB)		G13 M14 V15 R36 L41 A64 V66 G67 H179
Binding residue
(residue number reindexed from 1)		G11 M12 V13 R34 L39 A62 V64 G65 H177
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) S107 S108 C109 Y136 R140 H179
Catalytic site (residue number reindexed from 1) S105 S106 C107 Y134 R138 H177
Enzyme Commision number 1.1.1.271: GDP-L-fucose synthase.
Gene Ontology
Molecular Function
GO:0016491 oxidoreductase activity
GO:0016853 isomerase activity
GO:0042803 protein homodimerization activity
GO:0050577 GDP-L-fucose synthase activity
GO:0070401 NADP+ binding
Biological Process
GO:0009226 nucleotide-sugar biosynthetic process
GO:0009242 colanic acid biosynthetic process
GO:0042351 'de novo' GDP-L-fucose biosynthetic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1e7s, PDBe:1e7s, PDBj:1e7s
PDBsum1e7s
PubMed11021971
UniProtP32055|FCL_ECOLI GDP-L-fucose synthase (Gene Name=fcl)

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