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Structural and functional characterization of a 5,10- methenyltetrahydrofolate synthetase from mycoplasma pneumoniae (gi: 13508087)
Analyse Structural and functional characterization of a 5,10- methenyltetrahydrofolate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1U3G
- Type
- protein
- Length
- 164 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 5,10-methenyltetrahydrofolate synthetase
- EC
- 6.3.3.2
- UniProt
- P75430
- Ligands
- ADP, THF, MG, PO4
- Pockets
- 1 · best druggability 0.54
Structure
x-ray diffraction · 1 distinct chain · 31% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 5,10-methenyltetrahydrofolate synthetase (EC 6.3.3.2) | protein | 164 | 31% helix, 21% strand | P75430 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · chains A
- THF · 5-hydroxymethylene-6-hydrofolic acid · ligand · chains A
- MG · Magnesium ion · metal · chains A
- PO4 · Phosphate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 173 | 0.54 | 0.79 | 25 | PO4, MG, THF |
Compared structures
- 1U3G · Structural and Functional Characterization of a 5,10-Methenyltetrahydrofolate Synthetase… · the same entry in another collection · chain A against A, TM-score 1.00
- P75430 · AlphaFold monomer V2.0 prediction for 5-formyltetrahydrofolate cyclo- ligase (P75430) · a predicted model of the same protein · chain A against A, TM-score 0.99
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P75430
- Elsewhere: RCSB PDB 1U3G · PDBe 1U3G · UniProt P75430
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