Research workbench
60S ribosomal protein L8 histidine hydroxylase (NO66) in apo form
Analyse 60S ribosomal protein L8 histidine hydroxylase (NO66) in apo form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4CCJ
- Type
- protein
- Length
- 1,831 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bifunctional lysine-specific demethylase and histidyl- hydroxylase NO66
- EC
- 1.14.11.-, 1.14.11.27
- UniProt
- Q9H6W3
- Pockets
- 19 · best druggability 0.75
Structure
x-ray diffraction · 2 distinct chains · 37% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Bifunctional lysine-specific demethylase and histidyl- hydroxylase NO66 (EC 1.14.11.-, 1.14.11.27) | protein | 458 | 37% helix, 21% strand | Q9H6W3 |
| D | Bifunctional lysine-specific demethylase and histidyl- hydroxylase NO66 (EC 1.14.11.-, 1.14.11.27) | protein | 457 | 36% helix, 21% strand | Q9H6W3 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 3 copies · chains B, D, A, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
19 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 298 | 0.75 | 0.87 | 47 | empty |
| 2 | 940 | 0.73 | 0.77 | 103 | empty |
| 3 | 280 | 0.73 | 0.86 | 45 | empty |
| 4 | 257 | 0.70 | 0.85 | 39 | empty |
| 5 | 287 | 0.70 | 0.84 | 35 | empty |
Interfaces
4 interfaces between chains.
- B–D · 3387 Ų buried · 53 hydrogen bonds · protein-protein
- A–C · 3360 Ų buried · 55 hydrogen bonds · protein-protein
- A–B · 1267 Ų buried · 6 hydrogen bonds · protein-protein
- C–D · 1170 Ų buried · 6 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 Q9H6W3
- Elsewhere: RCSB PDB 4CCJ · PDBe 4CCJ · UniProt Q9H6W3
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