Research workbench
Crystal structure of emsy-HP1 complex
Analyse Crystal structure of emsy-HP1 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2FMM
- Type
- protein
- Length
- 386 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q7Z589, P83916
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| E | — | protein | 118 | — | Q7Z589 |
| A | — | protein | 68 | — | P83916 |
| B, C | — | protein | 67 | — | P83916 |
| D | — | protein | 66 | — | P83916 |
Compared structures
- 2FMM · Crystal Structure of EMSY-HP1 complex · the same entry in another collection · chain D against D, TM-score 1.00
- P83916 · AlphaFold monomer V2.0 prediction for chromobox protein homolog 1 (P83916) · a predicted model of the same protein · chain D against A, TM-score 0.93
- Q7Z589 · AlphaFold monomer V2.0 prediction for BRCA2-interacting transcriptional repressor emsy… · a predicted model of the same protein · chain E against A, TM-score 0.78
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 Q7Z589
- Every structure of UniProt P83916
- Elsewhere: RCSB PDB 2FMM · PDBe 2FMM · UniProt Q7Z589 · UniProt P83916
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