Structure of PDB 1hj6 Chain A Binding Site BS02

Receptor Information
>1hj6 Chain A (length=414) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SKVVVPAQGKKITLQNGKLNVPENPIIPYIEGDGIGVDVTPAMLKVVDAA
VEKAYKGERKISWMEIYTGEKSTQVYGQDVWLPAETLDLIREYRVAIKGP
LTTPVGGGIRELNVALRQELDLYICLRPVRYYQGTPSPVKHPELTDMVIF
RENSEDIYAGIEWKADSADAEKVIKFLREEMGVKKIRFPEHCGIGIKPCS
EEGTKRLVRAAIEYAIANDRDSVTLVHKGNIMKFTEGAFKDWGYQLAREE
FGGELIDGGPWLKVKNPNTGKEIVIKDVIADAFLQQILLRPAEYDVIACM
NLNGDYISDALAAQVGGIGIAPGANIGDECALFEATHGTAPKYAGQDKVN
PGSIILSAEMMLRHMGWTEAADLIVKGMEGAINAKTVTYDFERLMDGAKL
LKCSEFGDAIIENM
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 chain1hj6 Chain A Residue 1420 [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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PDB1hj6 Structural Basis for a Change in Substrate Specificity: Crystal Structure of S113E Isocitrate Dehydrogenase in a Complex with Isopropylmalate, Mg2+ and Nadp
Resolution2.0 Å
Binding residue
(original residue number in PDB)		P102 L103 T104 N115 I320 G321 H339 G340 T341 A342 Y345 V351 N352 Y391 D392
Binding residue
(residue number reindexed from 1)		P100 L101 T102 N113 I318 G319 H337 G338 T339 A340 Y343 V349 N350 Y389 D390
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) Y160 K230 D283 D307 D311
Catalytic site (residue number reindexed from 1) Y158 K228 D281 D305 D309
Enzyme Commision number 1.1.1.42: isocitrate dehydrogenase (NADP(+)).
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0004450 isocitrate dehydrogenase (NADP+) activity
GO:0005515 protein binding
GO:0016491 oxidoreductase activity
GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
GO:0046872 metal ion binding
GO:0051287 NAD binding
GO:0097216 guanosine tetraphosphate binding
Biological Process
GO:0006097 glyoxylate cycle
GO:0006099 tricarboxylic acid cycle
GO:0006979 response to oxidative stress
GO:0022900 electron transport chain
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function
View graph for
Biological Process
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Cellular Component
External links
PDB RCSB:1hj6, PDBe:1hj6, PDBj:1hj6
PDBsum1hj6
PubMed11284679
UniProtP08200|IDH_ECOLI Isocitrate dehydrogenase [NADP] (Gene Name=icd)

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