MolNFT v1 · #14826 · protein
Structure and catalytic mechanism of a set domain protein methyltransferase
1MLV: “Structure and catalytic mechanism of a set domain protein methyltransferase”. X-ray diffraction. MolNFT v1 #14826 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1MLV
- Type
- protein
- Length
- 1,305 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q43088
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 425 | — | Q43088 |
| B | — | protein | 441 | — | Q43088 |
| C | — | protein | 439 | — | Q43088 |
Compared structures
- 1MLV · Structure and Catalytic Mechanism of a SET Domain Protein Methyltransferase · the same entry in another collection · chain B against B, TM-score 1.00
- Q43088 · AlphaFold monomer V2.0 prediction for ribulose-1,5 bisphosphate CARBOXYLASE/OXYGENASE… · a predicted model of the same protein · chain C against A, TM-score 0.99
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 Q43088
- Elsewhere: RCSB PDB 1MLV · PDBe 1MLV · UniProt Q43088
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