Research workbench
WDR5 and unmodified histone H3 complex at 2.25 ångström
Analyse WDR5 and unmodified histone H3 complex at 2.25 ångström in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2CO0
- Type
- protein
- Length
- 618 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Wd-repeat protein 5; Histone H3 dimethyl-lysine 4
- UniProt
- P61964, Q5TEC6
- Pockets
- 4 · best druggability 0.73
Structure
x-ray diffraction · 3 distinct chains · 0% helix, 50% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Wd-repeat protein 5 | protein | 304 | 0% helix, 51% strand | P61964 |
| B, D | Histone H3 dimethyl-lysine 4 | protein | 5 | 0% helix, 0% strand | Q5TEC6 |
| C | Wd-repeat protein 5 | protein | 304 | 0% helix, 50% strand | P61964 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 508 | 0.73 | 0.82 | 44 | empty |
| 2 | 483 | 0.73 | 0.82 | 44 | empty |
| 3 | 79 | 0.33 | 0.75 | 14 | empty |
| 4 | 69 | 0.33 | 0.75 | 14 | empty |
Interfaces
3 interfaces between chains.
- A–C · 643 Ų buried · 13 hydrogen bonds · protein-protein
- C–D · 454 Ų buried · 6 hydrogen bonds · protein-protein
- A–B · 447 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
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 2CO0 · PDBe 2CO0 · UniProt P61964 · UniProt Q5TEC6
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