Research workbench
A. thaliana cobalamine independent methionine synthase
Analyse A. thaliana cobalamine independent methionine synthase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1U22
- Type
- protein
- Length
- 746 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
- O50008
- Ligands
- HCS, THG, ZN, SO4
- Pockets
- 11 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 5-methyltetrahydropteroyltriglutamate-- homocysteine methyltransferase (EC 2.1.1.14) | protein | 746 | 40% helix, 12% strand | O50008 |
Ligands and binding sites
- HCS · 2-amino-4-mercapto-butyric acid · ligand · chains A
- THG · (6S)-5,6,7,8-tetrahydrofolate · ligand · chains A
- ZN · Zinc ion · metal · 2 copies · chains A
- SO4 · Sulfate ion · ion · 4 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 602 | 0.73 | 0.81 | 61 | SO4 |
| 2 | 74 | 0.73 | 0.97 | 22 | empty |
| 3 | 571 | 0.64 | 0.75 | 50 | ZN, SO4, HCS, THG |
| 4 | 159 | 0.57 | 0.82 | 19 | empty |
| 5 | 132 | 0.57 | 0.83 | 18 | empty |
Modifications
Observed in the structure: 18 modified (engineered).
Compared structures
- 1U22 · A. thaliana cobalamine independent methionine synthase · the same entry in another collection · chain A against A, TM-score 1.00
- O50008 · AlphaFold monomer V2.0 prediction for 5-methyltetrahydropteroyltriglutamate--homocysteine… · 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 O50008
- Elsewhere: RCSB PDB 1U22 · PDBe 1U22 · UniProt O50008
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