MolNFT v1 · #23492 · protein
A. thaliana cobalamine independent methionine synthase
1U1U · 5-methyltetrahydropteroyltriglutamate-- homocysteine…: “A. thaliana cobalamine independent methionine synthase”. X-ray diffraction, 2 ligands (ZN, SO4), 12 pockets (best druggability 0.79). MolNFT v1 #23492 on GenesisL1: 3D…
- PDB
- 1U1U
- 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
- ZN, SO4
- Pockets
- 12 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 5-methyltetrahydropteroyltriglutamate-- homocysteine methyltransferase (EC 2.1.1.14) | protein | 746 | 36% helix, 11% strand | O50008 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 119 | 0.79 | 0.97 | 33 | empty |
| 2 | 1042 | 0.77 | 0.79 | 123 | ZN, SO4 |
| 3 | 139 | 0.72 | 0.91 | 39 | empty |
| 4 | 58 | 0.66 | 0.95 | 22 | empty |
| 5 | 66 | 0.65 | 0.93 | 22 | empty |
Modifications
Observed in the structure: 18 modified (engineered).
Compared structures
- 1U1U · 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 0.97
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 1U1U · PDBe 1U1U · UniProt O50008
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