Research workbench
10,5-methenyltetrahydrofolate cyclohydrolase from methylobacterium extorquens AM1 with tetrahydrofolate
Analyse 10,5-methenyltetrahydrofolate cyclohydrolase from methylobacterium extorquens… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7VG5
- Type
- protein
- Length
- 408 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Methenyltetrahydrofolate cyclohydrolase
- EC
- 3.5.4.9
- UniProt
- Q49135
- Ligands
- THG
- Pockets
- 3 · best druggability 0.59
Structure
x-ray diffraction · 1 distinct chain · 86% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Methenyltetrahydrofolate cyclohydrolase (EC 3.5.4.9) | protein | 204 | 86% helix, 0% strand | Q49135 |
Ligands and binding sites
- THG · (6S)-5,6,7,8-tetrahydrofolate · ligand · 2 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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 196 | 0.59 | 0.81 | 34 | THG |
| 2 | 167 | 0.57 | 0.81 | 34 | THG |
| 3 | 59 | 0.43 | 0.82 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 2307 Ų buried · 18 hydrogen bonds · protein-protein
Compared structures
- 7VG5 · 10,5-methenyltetrahydrofolate cyclohydrolase from Methylobacterium extorquens AM1 with… · the same entry in another collection · chain A against A, TM-score 1.00
- Q49135 · AlphaFold monomer V2.0 prediction for methenyltetrahydrofolate cyclohydrolase (Q49135) · 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 Q49135
- Elsewhere: RCSB PDB 7VG5 · PDBe 7VG5 · UniProt Q49135
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