Structure of PDB 1u3g Chain A Binding Site BS01

Receptor Information
>1u3g Chain A (length=164) Species: 2104 (Mycoplasmoides pneumoniae) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MDKNALRKQILQKRMALSTIEKSHLDQKINQKLVAFLTPKPCIKTIALYE
PIKNEVTFVDFFFEFLKINQIRAVYPKVISDTEIIFIDQETNTFEPNQID
CFLIPLVGFNKDNYRLGFGKGYYDRYLMQLTRQQPKIGIAYSFQKGDFLA
DPWDVQLDLIINDE
Ligand information
Ligand IDMG
InChIInChI=1S/Mg/q+2
InChIKeyJLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mg+2]
CACTVS 3.341[Mg++]
FormulaMg
NameMAGNESIUM ION
ChEMBL
DrugBankDB01378
ZINC
PDB chain1u3g Chain A Residue 401 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1u3g Crystal structure of methenyltetrahydrofolate synthetase from Mycoplasma pneumoniae (GI: 13508087) at 2.2 A resolution
Resolution2.5 Å
Binding residue
(original residue number in PDB)
D124 D154
Binding residue
(residue number reindexed from 1)
D124 D154
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) R115 D124 D154
Catalytic site (residue number reindexed from 1) R115 D124 D154
Enzyme Commision number 6.3.3.2: 5-formyltetrahydrofolate cyclo-ligase.
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0016874 ligase activity
GO:0030272 5-formyltetrahydrofolate cyclo-ligase activity
GO:0046872 metal ion binding
Biological Process
GO:0009396 folic acid-containing compound biosynthetic process
GO:0035999 tetrahydrofolate interconversion
Cellular Component
GO:0005737 cytoplasm

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Biological Process

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Cellular Component
External links
PDB RCSB:1u3g, PDBe:1u3g, PDBj:1u3g
PDBsum1u3g
PubMed15281135
UniProtP75430|MTHFS_MYCPN 5-formyltetrahydrofolate cyclo-ligase (Gene Name=MPN_348)

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