Structure of PDB 1t6x Chain A Binding Site BS01

Receptor Information
>1t6x Chain A (length=266) Species: 2336 (Thermotoga maritima) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
VVSIGVFDGVHIGHQKVLRTMKEIAFFRKDDSLIYTISYPPEYFLPDFPG
LLMTVESRVEMLSRYARTVVLDFFRIKDLTPEGFVERYLSGVSAVVVGRD
FRFGKNASGNASFLRKKGVEVYEIEDVVVQGKRVSSSLIRNLVQEGRVEE
IPAYLGRYFEIEGIVFPTANIDRGNEKLVDLKRGVYLVRVHLPDGKKKFG
VMNVGFRRNVKYEVYILDFEGDLYGQRLKLEVLKFMRDEKKEELKAAIDQ
DVKSARNMIDDIINSK
Ligand information
Ligand IDADP
InChIInChI=1S/C10H15N5O10P2/c11-8-5-9(13-2-12-8)15(3-14-5)10-7(17)6(16)4(24-10)1-23-27(21,22)25-26(18,19)20/h2-4,6-7,10,16-17H,1H2,(H,21,22)(H2,11,12,13)(H2,18,19,20)/t4-,6-,7-,10-/m1/s1
InChIKeyXTWYTFMLZFPYCI-KQYNXXCUSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@](=O)(O)OP(=O)(O)O)O)O)N
CACTVS 3.341Nc1ncnc2n(cnc12)[CH]3O[CH](CO[P](O)(=O)O[P](O)(O)=O)[CH](O)[CH]3O
ACDLabs 10.04O=P(O)(O)OP(=O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3O
CACTVS 3.341Nc1ncnc2n(cnc12)[C@@H]3O[C@H](CO[P@@](O)(=O)O[P](O)(O)=O)[C@@H](O)[C@H]3O
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)OP(=O)(O)O)O)O)N
FormulaC10 H15 N5 O10 P2
NameADENOSINE-5'-DIPHOSPHATE
ChEMBLCHEMBL14830
DrugBankDB16833
ZINCZINC000012360703
PDB chain1t6x Chain A Residue 294 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1t6x Crystal structure of ADP bound FAD synthetase
Resolution2.29 Å
Binding residue
(original residue number in PDB)		P179 T180 A181 N182 I234 G239 L241 Y242
Binding residue
(residue number reindexed from 1)		P167 T168 A169 N170 I216 G221 L223 Y224
Annotation score5
Enzymatic activity
Enzyme Commision number 2.7.1.26: riboflavin kinase.
2.7.7.2: FAD synthase.
Gene Ontology
Molecular Function
GO:0003919 FMN adenylyltransferase activity
GO:0005524 ATP binding
GO:0008531 riboflavin kinase activity
GO:0016301 kinase activity
GO:0016779 nucleotidyltransferase activity
GO:0046872 metal ion binding
Biological Process
GO:0006747 FAD biosynthetic process
GO:0006771 riboflavin metabolic process
GO:0009231 riboflavin biosynthetic process
GO:0009398 FMN biosynthetic process
GO:0016310 phosphorylation

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Molecular Function
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Biological Process
External links
PDB RCSB:1t6x, PDBe:1t6x, PDBj:1t6x
PDBsum1t6x
PubMed
UniProtQ9WZW1

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