Research workbench
Crystal structure of the candida albicans methionine synthase in complex with homocysteine
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
- 4L5Z
- Type
- protein
- Length
- 753 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
- HCS, ZN
- Pockets
- 8 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 46% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase (EC 2.1.1.14) | protein | 753 | 46% helix, 14% strand | P82610 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 97 | 0.77 | 0.98 | 23 | empty |
| 2 | 1113 | 0.76 | 0.78 | 106 | ZN, HCS |
| 3 | 244 | 0.65 | 0.83 | 28 | empty |
| 4 | 247 | 0.57 | 0.78 | 40 | empty |
| 5 | 71 | 0.47 | 0.83 | 20 | empty |
Compared structures
- 4L5Z · Crystal structure of the Candida albicans Methionine Synthase in complex with Homocysteine · 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 4L5Z · PDBe 4L5Z · UniProt P82610
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