Structure of PDB 1xaj Chain A Binding Site BS02

Receptor Information
>1xaj Chain A (length=337) Species: 1280 (Staphylococcus aureus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MKLQTTYPSNNYPIYVEHGAIKYIGTYLNQFDQSFLLIDEYVNQYFANKF
DDINVHKVIIPAGEKTKTFEQYQETLEYILSHHVTRNTAIIAVGGGATGD
FAGFVAATLLRGVHFIQVPTTILAHDSSVGGKVGINSKQGKNLIGAFYRP
TAVIYDLDFLKTLPFKQILSGYAEVYKHALLNGESATQDIEQHFKDREIL
QSLNGMDKYIAKGIETKLDIVVADEKEQGVRKFLNLGHTFGHAVEYYHKI
PHGHAVMVGIIYQFIVANALFDSKHDISHYIQYLIQLGYPLDMYMLSDKK
NDKQGVQMVLMRQFGDIVVQHVDQLTLQHACEQLKTY
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 chain1xaj Chain A Residue 400 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1xaj Comparison of ligand induced conformational changes and domain closure mechanisms, between prokaryotic and eukaryotic dehydroquinate synthases.
Resolution2.35 Å
Binding residue
(original residue number in PDB)		D39 Y41 V42 G67 E68 K71 G99 G100 A101 D104 T124 T125 L127 D130 S131 K136 K145 T166 L167 Q171
Binding residue
(residue number reindexed from 1)		D39 Y41 V42 G63 E64 K67 G95 G96 A97 D100 T120 T121 L123 D126 S127 K132 K141 T162 L163 Q167
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) R111 K132 E174 K217 E227 R231 N235 H238 H242 H252
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:1xaj, PDBe:1xaj, PDBj:1xaj
PDBsum1xaj
PubMed15465043
UniProtQ6GGU4|AROB_STAAR 3-dehydroquinate synthase (Gene Name=aroB)

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