Structure of PDB 1gll Chain Y Binding Site BS01

Receptor Information
>1gll Chain Y (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 IDACP
InChIInChI=1S/C11H18N5O12P3/c12-9-6-10(14-2-13-9)16(3-15-6)11-8(18)7(17)5(27-11)1-26-31(24,25)28-30(22,23)4-29(19,20)21/h2-3,5,7-8,11,17-18H,1,4H2,(H,22,23)(H,24,25)(H2,12,13,14)(H2,19,20,21)/t5-,7-,8-,11-/m1/s1
InChIKeyUFZTZBNSLXELAL-IOSLPCCCSA-N
SMILES
SoftwareSMILES
CACTVS 3.341Nc1ncnc2n(cnc12)[CH]3O[CH](CO[P](O)(=O)O[P](O)(=O)C[P](O)(O)=O)[CH](O)[CH]3O
ACDLabs 10.04O=P(O)(O)CP(=O)(O)OP(=O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3O
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)OP(=O)(CP(=O)(O)O)O)O)O)N
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)(CP(=O)(O)O)O)O)O)N
CACTVS 3.341Nc1ncnc2n(cnc12)[C@@H]3O[C@H](CO[P@](O)(=O)O[P@](O)(=O)C[P](O)(O)=O)[C@@H](O)[C@H]3O
FormulaC11 H18 N5 O12 P3
NamePHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER;
ADENOSINE-5'-[BETA, GAMMA-METHYLENE]TRIPHOSPHATE
ChEMBLCHEMBL133463
DrugBankDB03909
ZINCZINC000008295124
PDB chain1gll Chain Y 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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PDB1gll 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)		G12 T13 T14 T267 G310 I313 A326 S329 G411
Binding residue
(residue number reindexed from 1)		G11 T12 T13 T262 G305 I308 A321 S324 G406
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:1gll, PDBe:1gll, PDBj:1gll
PDBsum1gll
PubMed10090737
UniProtP0A6F3|GLPK_ECOLI Glycerol kinase (Gene Name=glpK)

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