Research workbench
Crystal Structure of methenyltetrahydrofolate synthetase from Mycoplasma pneumoniae at 2.2 resolution
Analyse Crystal Structure of methenyltetrahydrofolate synthetase from Mycoplasma… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1SBQ
- Type
- protein
- Length
- 328 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.2
- Source
- Mycoplasma pneumoniae
- Molecule
- 5,10-Methenyltetrahydrofolate synthetase homolog
- EC
- 6.3.3.2
- UniProt
- P75430
- Ligands
- SO4
- Pockets
- 3 · best druggability 0.48
Structure
x-ray diffraction · resolution 2.2 · 1 distinct chain · 34% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | 5,10-Methenyltetrahydrofolate synthetase homolog (EC 6.3.3.2) | protein | 164 | 34% helix, 21% strand | P75430 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 142 | 0.48 | 0.77 | 17 | SO4 |
| 2 | 145 | 0.46 | 0.77 | 21 | empty |
| 3 | 128 | 0.43 | 0.76 | 21 | SO4 |
Interfaces
1 interface between chains.
- A–B · 406 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 1SBQ · Crystal structure of methenyltetrahydrofolate synthetase from mycoplasma pneumoniae at… · 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 0.98
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 1SBQ · PDBe 1SBQ · UniProt P75430
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