Research workbench
Crystal structure of human WDR5 in complex with monomethyl L-arginine
Analyse Crystal structure of human WDR5 in complex with monomethyl L-arginine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6OI1
- Type
- protein
- Length
- 304 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Wd repeat-containing protein 5
- UniProt
- P61964
- Ligands
- NMM, SO4
- Pockets
- 1 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 0% helix, 51% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Wd repeat-containing protein 5 | protein | 304 | 0% helix, 51% strand | P61964 |
Ligands and binding sites
- NMM · (2S)-2-amino-5-[(N-methylcarbamimidoyl)amino]pentanoic acid · ligand · chains A
- SO4 · Sulfate ion · ion · chains A
- GOL · Glycerol · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 646 | 0.75 | 0.81 | 64 | SO4, NMM |
Compared structures
- 6OI1 · Crystal structure of human WDR5 in complex with monomethyl L-arginine · the same entry in another collection · chain A against A, TM-score 1.00
- P61964 · AlphaFold monomer V2.0 prediction for wd repeat-containing protein 5 (P61964) · a predicted model of the same protein · 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
- Elsewhere: RCSB PDB 6OI1 · PDBe 6OI1 · UniProt P61964
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