Structure of PDB 2ogy Chain B Binding Site BS02

Receptor Information
>2ogy Chain B (length=262) Species: 1525 (Moorella thermoacetica) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MLIIGERINGMFGDIKRAIQERDPAPVQEWARRQEEGGARALDLNVGPAV
QDKVSAMEWLVEVTQEVSNLTLCLDSTNIKAIEAGLKKCKNRAMINSTNA
EREKVEKLFPLAVEHGAALIGLTMNKTGIPKDSDTRLAFAMELVAAADEF
GLPMEDLYIDPLILPANVAQDHAPEVLKTLQQIKMLADPAPKTVLGLSAV
SQNCQNRPLINRTFLAMAMACGLDAAIADACDEALIETAATAEILLNQTV
YCDSFVKMFKTR
Ligand information
Ligand IDC2F
InChIInChI=1S/C20H25N7O6/c1-27-12(9-23-16-15(27)18(31)26-20(21)25-16)8-22-11-4-2-10(3-5-11)17(30)24-13(19(32)33)6-7-14(28)29/h2-5,12-13,22H,6-9H2,1H3,(H,24,30)(H,28,29)(H,32,33)(H4,21,23,25,26,31)/t12-,13-/m0/s1
InChIKeyZNOVTXRBGFNYRX-STQMWFEESA-N
SMILES
SoftwareSMILES
CACTVS 3.341CN1[CH](CNc2ccc(cc2)C(=O)N[CH](CCC(O)=O)C(O)=O)CNC3=C1C(=O)NC(=N3)N
ACDLabs 10.04O=C(O)C(NC(=O)c1ccc(cc1)NCC2N(C=3C(=O)NC(=NC=3NC2)N)C)CCC(=O)O
OpenEye OEToolkits 1.5.0CN1C(CNC2=C1C(=O)NC(=N2)N)CNc3ccc(cc3)C(=O)NC(CCC(=O)O)C(=O)O
OpenEye OEToolkits 1.5.0C[N@@]1[C@H](CNC2=C1C(=O)NC(=N2)N)CNc3ccc(cc3)C(=O)N[C@@H](CCC(=O)O)C(=O)O
CACTVS 3.341CN1[C@@H](CNc2ccc(cc2)C(=O)N[C@@H](CCC(O)=O)C(O)=O)CNC3=C1C(=O)NC(=N3)N
FormulaC20 H25 N7 O6
Name5-METHYL-5,6,7,8-TETRAHYDROFOLIC ACID
ChEMBLCHEMBL1231574
DrugBankDB11256
ZINCZINC000002005305
PDB chain2ogy Chain B Residue 4000 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB2ogy Structural and kinetic evidence for an extended hydrogen-bonding network in catalysis of methyl group transfer. Role of an active site asparagine residue in activation of methyl transfer by methyltransferases.
Resolution2.3 Å
Binding residue
(original residue number in PDB)		M11 F12 D75 N96 D160 G196 S198 Q202 R207
Binding residue
(residue number reindexed from 1)		M11 F12 D75 N96 D160 G196 S198 Q202 R207
Annotation score4
Binding affinityMOAD: Kd=33.2uM
Enzymatic activity
Enzyme Commision number 2.1.1.258: 5-methyltetrahydrofolate:corrinoid/iron-sulfur protein Co-methyltransferase.
Gene Ontology
Molecular Function
GO:0005509 calcium ion binding
GO:0005515 protein binding
GO:0008168 methyltransferase activity
GO:0008705 methionine synthase activity
GO:0031419 cobalamin binding
GO:0046872 metal ion binding
GO:0102036 methyltetrahydrofolate:corrinoid/iron-sulfur protein methyltransferase activity
Biological Process
GO:0009086 methionine biosynthetic process
GO:0015977 carbon fixation
GO:0032259 methylation
GO:0042558 pteridine-containing compound metabolic process
GO:0044237 cellular metabolic process
Cellular Component
GO:0005829 cytosol

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:2ogy, PDBe:2ogy, PDBj:2ogy
PDBsum2ogy
PubMed17172470
UniProtQ46389|ACSE_MOOTH 5-methyltetrahydrofolate:corrinoid/iron-sulfur protein co-methyltransferase (Gene Name=acsE)

[Back to BioLiP]