Research workbench
Crystal structure of the candida albicans methionine synthase by surface entropy reduction, alanine variant with zinc
Analyse Crystal structure of the candida albicans methionine synthase by surface… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3PPG
- Type
- protein
- Length
- 740 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
- ZN
- Pockets
- 12 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 48% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase (EC 2.1.1.14) | protein | 740 | 48% helix, 14% strand | P82610 |
Ligands and binding sites
- ZN · Zinc ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 105 | 0.78 | 0.98 | 25 | empty |
| 2 | 631 | 0.73 | 0.80 | 56 | empty |
| 3 | 323 | 0.60 | 0.77 | 44 | empty |
| 4 | 186 | 0.58 | 0.81 | 20 | empty |
| 5 | 85 | 0.52 | 0.84 | 20 | empty |
Compared structures
- 3PPG · Crystal structure of the Candida albicans methionine synthase by surface entropy… · 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 0.95
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 3PPG · PDBe 3PPG · UniProt P82610
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