Structure of PDB 1xah Chain B Binding Site BS02

Receptor Information
>1xah Chain B (length=330) Species: 1280 (Staphylococcus aureus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MKLQTTYPSNNYPIYVEHGAIKYIGTYLNQFDQSFLLIDEYVNQYFANKF
DNVHKVIIPAGEKTKTFEQYQETLEYILSHHVTRNTAIIAVGGGATGDFA
GFVAATLLRGVHFIQVPTTILAHDSSVGGKVGINSKQGKNLIGAFYRPTA
VIYDLDFLKTLPFKQILSGYAEVYKHALLNGESATQDIEQHFKDREILQS
LNGMDKYIAKGIETKLDIVVADEKEQGVRKFLNLGHTFGHAVEYYHKIPH
GHAVMVGIIYQFIVANALFDSKHDISHYIQYLIQLGYPLDTLYQYMLGVQ
MVLMRQFGDIVVQHVDQLTLQHACEQLKTY
Ligand information
Ligand IDNAD
InChIInChI=1S/C21H27N7O14P2/c22-17-12-19(25-7-24-17)28(8-26-12)21-16(32)14(30)11(41-21)6-39-44(36,37)42-43(34,35)38-5-10-13(29)15(31)20(40-10)27-3-1-2-9(4-27)18(23)33/h1-4,7-8,10-11,13-16,20-21,29-32H,5-6H2,(H5-,22,23,24,25,33,34,35,36,37)/t10-,11-,13-,14-,15-,16-,20-,21-/m1/s1
InChIKeyBAWFJGJZGIEFAR-NNYOXOHSSA-N
SMILES
SoftwareSMILES
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)[C@@H]3O)n4cnc5c(N)ncnc45)[C@@H](O)[C@H]2O
OpenEye OEToolkits 1.5.0c1cc(c[n+](c1)C2C(C(C(O2)COP(=O)([O-])OP(=O)(O)OCC3C(C(C(O3)n4cnc5c4ncnc5N)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)[CH]3O)n4cnc5c(N)ncnc45)[CH](O)[CH]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)O)O)O)O)C(=O)N
FormulaC21 H27 N7 O14 P2
NameNICOTINAMIDE-ADENINE-DINUCLEOTIDE
ChEMBLCHEMBL1234613
DrugBankDB14128
ZINC
PDB chain1xah Chain B Residue 401 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1xah Comparison of ligand induced conformational changes and domain closure mechanisms, between prokaryotic and eukaryotic dehydroquinate synthases.
Resolution2.2 Å
Binding residue
(original residue number in PDB)		D39 Y41 V42 Y45 E68 K71 G99 G100 A101 D104 T124 T125 L127 D130 S131 K136 K145 F163 T166 L167 Q171
Binding residue
(residue number reindexed from 1)		D39 Y41 V42 Y45 E62 K65 G93 G94 A95 D98 T118 T119 L121 D124 S125 K130 K139 F157 T160 L161 Q165
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) R115 K136 E178 K221 E231 R235 N239 H242 H246 H256
Catalytic site (residue number reindexed from 1) R109 K130 E172 K215 E225 R229 N233 H236 H240 H250
Enzyme Commision number 4.2.3.4: 3-dehydroquinate synthase.
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0003856 3-dehydroquinate synthase activity
GO:0016829 lyase activity
GO:0016838 carbon-oxygen lyase activity, acting on phosphates
GO:0046872 metal ion binding
Biological Process
GO:0008652 amino acid biosynthetic process
GO:0009073 aromatic amino acid family biosynthetic process
GO:0009423 chorismate 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:1xah, PDBe:1xah, PDBj:1xah
PDBsum1xah
PubMed15465043
UniProtQ6GGU4|AROB_STAAR 3-dehydroquinate synthase (Gene Name=aroB)

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