Research workbench
Structure of the C-terminal domain of the saccharomyces cerevisiae mutl alpha (MLH1/PMS1) heterodimer
Analyse Structure of the C-terminal domain of the saccharomyces cerevisiae mutl alpha… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4E4W
- Type
- protein
- Length
- 474 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P38920, P14242
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 261 | — | P38920 |
| B | — | protein | 213 | — | P14242 |
Compared structures
- 4E4W · Structure of the C-terminal domain of the Saccharomyces cerevisiae MUTL alpha (MLH1/PMS1)… · the same entry in another collection · chain A against A, TM-score 1.00
- P38920 · AlphaFold monomer V2.0 prediction for DNA mismatch repair protein MLH1 (P38920) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 P38920
- Every structure of UniProt P14242
- Elsewhere: RCSB PDB 4E4W · PDBe 4E4W · UniProt P38920 · UniProt P14242
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