Research workbench
Crystal structure of the tetramerisation domain of human ctip
Analyse Crystal structure of the tetramerisation domain of human ctip in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4D2H
- Type
- protein
- Length
- 268 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- RBBP8
- EC
- 3.1.-.-
- UniProt
- Q99708
- Ligands
- SO4
- Pockets
- 2 · best druggability 0.37
Structure
x-ray diffraction · 7 distinct chains · 89% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | RBBP8 (EC 3.1.-.-) | protein | 37 | 92% helix, 0% strand | Q99708 |
| B | RBBP8 (EC 3.1.-.-) | protein | 32 | 88% helix, 0% strand | Q99708 |
| C | RBBP8 (EC 3.1.-.-) | protein | 34 | 94% helix, 0% strand | Q99708 |
| D, E | RBBP8 (EC 3.1.-.-) | protein | 30 | 93% helix, 0% strand | Q99708 |
| F | RBBP8 (EC 3.1.-.-) | protein | 37 | 86% helix, 0% strand | Q99708 |
| G | RBBP8 (EC 3.1.-.-) | protein | 35 | 80% helix, 0% strand | Q99708 |
| H | RBBP8 (EC 3.1.-.-) | protein | 33 | 94% helix, 0% strand | Q99708 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 14 copies · chains A, B, C, D, E, G, H, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 57 | 0.37 | 0.79 | 15 | SO4 |
| 2 | 50 | 0.28 | 0.75 | 14 | empty |
Interfaces
13 interfaces between chains.
- G–H · 702 Ų buried · 6 hydrogen bonds · protein-protein
- E–F · 616 Ų buried · 4 hydrogen bonds · protein-protein
- C–D · 611 Ų buried · 5 hydrogen bonds · protein-protein
- A–B · 602 Ų buried · 3 hydrogen bonds · protein-protein
- A–F · 525 Ų buried · 4 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 Q99708
- Elsewhere: RCSB PDB 4D2H · PDBe 4D2H · UniProt Q99708
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