Structure of PDB 1bwf Chain O Binding Site BS01

Receptor Information
>1bwf Chain O (length=494) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
EKKYIVALDQGTTSSRAVVMDHDANIISVSQREFEQIYPKPGWVEHDPME
IWATQSWTLVEVLAKADISSDQIAAIGITNQRETTIVWEKETGKPIYNAI
VWQCRRTAEICEHLKRDGLEDYIRSNTGLVIDPYFSGTKVKWILDHVEGS
RERARRGELLFGTVDTWLIWKMTQGRVHVTDYTNASRTMLFNIHTLDWDD
KMLEVLDIPREMLPEVRRSSEVYGQTNIGTRIPISGIAGDQQAALFGQLC
VKEGMAKNTYGTGCFMLMNTGEKAVKSENGLLTTIACGPTGEVNYALEGA
VFMAGASIQWLRDEMKLINDAYDSEYFATKVQNTNGVYVVPAFTGLGAPY
WDPYARGAIFGLTRGVNANHIIRATLESIAYQTRDVLEAMQADSGIRLHA
LRVDGGAVANNFLMQFQSDILGTRVERPEVREVTALGAAYLAGLAVGFWQ
NLDELQEKAVIEREFRPGIETTERNYRYAGWKKAVKRAMAWEEH
Ligand information
Ligand IDATF
InChIInChI=1S/C11H16F2N5O12P3/c12-11(13,31(21,22)23)32(24,25)30-33(26,27)28-1-4-6(19)7(20)10(29-4)18-3-17-5-8(14)15-2-16-9(5)18/h2-4,6-7,10,19-20H,1H2,(H,24,25)(H,26,27)(H2,14,15,16)(H2,21,22,23)/t4-,6-,7-,10-/m1/s1
InChIKeyODWAWOIUPXBZKQ-KQYNXXCUSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)OP(=O)(C(F)(F)P(=O)(O)O)O)O)O)N
ACDLabs 10.04FC(F)(P(=O)(O)O)P(=O)(O)OP(=O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3O
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@@](=O)(O)O[P@@](=O)(C(F)(F)P(=O)(O)O)O)O)O)N
CACTVS 3.341Nc1ncnc2n(cnc12)[CH]3O[CH](CO[P](O)(=O)O[P](O)(=O)C(F)(F)[P](O)(O)=O)[CH](O)[CH]3O
CACTVS 3.341Nc1ncnc2n(cnc12)[C@@H]3O[C@H](CO[P@](O)(=O)O[P@@](O)(=O)C(F)(F)[P](O)(O)=O)[C@@H](O)[C@H]3O
FormulaC11 H16 F2 N5 O12 P3
NamePHOSPHODIFLUOROMETHYLPHOSPHONIC ACID-ADENYLATE ESTER
ChEMBLCHEMBL1160358
DrugBank
ZINCZINC000015501787
PDB chain1bwf Chain O Residue 601 [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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PDB1bwf Crystal structures of Escherichia coli glycerol kinase variant S58-->W in complex with nonhydrolyzable ATP analogues reveal a putative active conformation of the enzyme as a result of domain motion.
Resolution3.0 Å
Binding residue
(original residue number in PDB)		T13 T14 T267 G310 I313 Q314 A326 G411 N415
Binding residue
(residue number reindexed from 1)		T12 T13 T262 G305 I308 Q309 A321 G406 N410
Annotation score3
Enzymatic activity
Enzyme Commision number 2.7.1.30: glycerol kinase.
Gene Ontology
Molecular Function
GO:0004370 glycerol kinase activity
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0008270 zinc ion binding
GO:0016301 kinase activity
GO:0016773 phosphotransferase activity, alcohol group as acceptor
GO:0042802 identical protein binding
GO:0046872 metal ion binding
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0006071 glycerol metabolic process
GO:0006072 glycerol-3-phosphate metabolic process
GO:0006974 DNA damage response
GO:0016310 phosphorylation
GO:0019563 glycerol catabolic process
Cellular Component
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1bwf, PDBe:1bwf, PDBj:1bwf
PDBsum1bwf
PubMed10090737
UniProtP0A6F3|GLPK_ECOLI Glycerol kinase (Gene Name=glpK)

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