Research workbench
Crystal structure of 3-methyl-2-oxobutanoate hydroxymethyltransferase
Analyse Crystal structure of 3-methyl-2-oxobutanoate hydroxymethyltransferase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1O68
- Type
- protein
- Length
- 1,269 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q9JZW6
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 250 | — | Q9JZW6 |
| B, D | — | protein | 262 | — | Q9JZW6 |
| C | — | protein | 246 | — | Q9JZW6 |
| E | — | protein | 249 | — | Q9JZW6 |
Compared structures
- 1O68 · Crystal structure of 3-methyl-2-oxobutanoate hydroxymethyltransferase · the same entry in another collection · chain A against A, TM-score 1.00
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 Q9JZW6
- Elsewhere: RCSB PDB 1O68 · PDBe 1O68 · UniProt Q9JZW6
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