Research workbench
Crystal structure of the candida albicans methionine synthase in complex with 5-methyl-tetrahydrofolate and methionine
Analyse Crystal structure of the candida albicans methionine synthase in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4L65
- Type
- protein
- Length
- 750 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase
- EC
- 2.1.1.14
- UniProt
- P82610
- Ligands
- C2F, MET, ZN
- Pockets
- 10 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 47% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase (EC 2.1.1.14) | protein | 750 | 47% helix, 14% strand | P82610 |
Ligands and binding sites
- C2F · 5-methyl-5,6,7,8-tetrahydrofolic acid · ligand · chains A
- MET · Methionine · ligand · chains A
- ZN · Zinc ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1148 | 0.79 | 0.80 | 116 | C2F, MET |
| 2 | 89 | 0.76 | 0.97 | 21 | empty |
| 3 | 338 | 0.66 | 0.80 | 41 | empty |
| 4 | 154 | 0.64 | 0.85 | 36 | empty |
| 5 | 71 | 0.50 | 0.84 | 20 | empty |
Compared structures
- 4L65 · Crystal structure of the Candida albicans Methionine Synthase in complex with… · the same entry in another collection · chain A against A, TM-score 1.00
- P82610 · AlphaFold monomer V2.0 prediction for 5-methyltetrahydropteroyltriglutamate--homocysteine… · a predicted model of the same protein · chain A against A, TM-score 0.96
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 P82610
- Elsewhere: RCSB PDB 4L65 · PDBe 4L65 · UniProt P82610
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