Research workbench
WDR5 and histone H3 lysine 4 dimethyl complex at 2.1 ångström
Analyse WDR5 and histone H3 lysine 4 dimethyl complex at 2.1 ångström in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2CNX
- Type
- protein
- Length
- 311 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P61964, Q5TEC6
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 306 | — | P61964 |
| P | — | protein | 5 | — | Q5TEC6 |
Compared structures
- 2CNX · WDR5 and Histone H3 Lysine 4 dimethyl complex at 2.1 angstrom · 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 P61964
- Every structure of UniProt Q5TEC6
- Elsewhere: RCSB PDB 2CNX · PDBe 2CNX · UniProt P61964 · UniProt Q5TEC6
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