Structure of PDB 2fmn Chain A Binding Site BS02

Receptor Information
>2fmn Chain A (length=288) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
FFHASQRDALNQSLAEVQGQINVSFEFFPPRTSEMEQTLWNSIDRLSSLK
PKFVSVTYGANSGERDRTHSIIKGIKDRTGLEAAPHLTCIDATPDELRTI
ARDYWNNGIRHIVALRGDLPPEMYASDLVTLLKEVADFDISVAAYPEVHP
EAKSAQADLLNLKRKVDAGVNRAITQFFFDVESYLRFRDRCVSAGIDVEI
IPGILPVSNFKQAKKFADMTNVRIPAWMAQMFDGLDDDAETRKLVGANIA
MDMVKILSREGVKDFHFYTLNRAEMSYAICHTLGVRPG
Ligand information
Ligand ID4HF
InChIInChI=1S/C19H23N5O6S/c20-19-23-15-11(16(27)24-19)7-9(8-21-15)1-2-10-3-5-13(31-10)17(28)22-12(18(29)30)4-6-14(25)26/h3,5,9,12H,1-2,4,6-8H2,(H,22,28)(H,25,26)(H,29,30)(H4,20,21,23,24,27)/t9-,12+/m1/s1
InChIKeyGQCXGHHHNACOGE-SKDRFNHKSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04O=C(O)C(NC(=O)c1sc(cc1)CCC3CNC=2N=C(N)NC(=O)C=2C3)CCC(=O)O
CACTVS 3.341NC1=NC2=C(C[C@@H](CCc3sc(cc3)C(=O)N[C@@H](CCC(O)=O)C(O)=O)CN2)C(=O)N1
OpenEye OEToolkits 1.5.0c1cc(sc1CCC2CC3=C(NC2)N=C(NC3=O)N)C(=O)NC(CCC(=O)O)C(=O)O
OpenEye OEToolkits 1.5.0c1cc(sc1CC[C@@H]2CC3=C(NC2)N=C(NC3=O)N)C(=O)N[C@@H](CCC(=O)O)C(=O)O
CACTVS 3.341NC1=NC2=C(C[CH](CCc3sc(cc3)C(=O)N[CH](CCC(O)=O)C(O)=O)CN2)C(=O)N1
FormulaC19 H23 N5 O6 S
NameN-[(5-{2-[(6R)-2-AMINO-4-OXO-3,4,5,6,7,8-HEXAHYDROPYRIDO[2,3-D]PYRIMIDIN-6-YL]ETHYL}-2-THIENYL)CARBONYL]-L-GLUTAMIC ACID;
6R-2',5'-THIENYL-5,10-DIDEAZATETRAHYDROFOLIC ACID;
LY309887
ChEMBL
DrugBank
ZINC
PDB chain2fmn Chain A Residue 495 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2fmn Structural Perturbations in the Ala -> Val Polymorphism of Methylenetetrahydrofolate Reductase: How Binding of Folates May Protect against Inactivation
Resolution2.05 Å
Binding residue
(original residue number in PDB)		D120 Q183 L212 Q219 F223 Y275 L277
Binding residue
(residue number reindexed from 1)		D118 Q176 L205 Q212 F216 Y268 L270
Annotation score2
Binding affinityMOAD: Ki~20uM
Enzymatic activity
Catalytic site (original residue number in PDB) S26 E28 D120 F223 H273
Catalytic site (residue number reindexed from 1) S24 E26 D118 F216 H266
Enzyme Commision number 1.5.1.54: methylenetetrahydrofolate reductase (NADH).
Gene Ontology
Molecular Function
GO:0004489 methylenetetrahydrofolate reductase (NAD(P)H) activity
GO:0016491 oxidoreductase activity
GO:0051087 protein-folding chaperone binding
GO:0071949 FAD binding
GO:0106312 methylenetetrahydrofolate reductase (NADH) activity
Biological Process
GO:0006555 methionine metabolic process
GO:0009086 methionine biosynthetic process
GO:0035999 tetrahydrofolate interconversion
Cellular Component
GO:0005829 cytosol
GO:0032991 protein-containing complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2fmn, PDBe:2fmn, PDBj:2fmn
PDBsum2fmn
PubMed16605249
UniProtP0AEZ1|METF_ECOLI 5,10-methylenetetrahydrofolate reductase (Gene Name=metF)

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