Research workbench
Crystal structure analysis of the clathrin trimerization domain
Analyse Crystal structure analysis of the clathrin trimerization domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3QIL
- Type
- protein
- Length
- 2,776 residues
- Chains
- 24
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Clathrin heavy chain 1
- UniProt
- P49951
- Pockets
- 20 · best druggability 0.85
Structure
x-ray diffraction · 2 distinct chains · 47% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, D, F, G, I, J, L, M, O, P, R, S, U, V, X | Clathrin heavy chain 1 | protein | 125 | 38% helix, 0% strand | P49951 |
| B, E, H, K, N, Q, T, W | Clathrin heavy chain 1 | protein | 97 | 60% helix, 0% strand | P49951 |
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1132 | 0.85 | 0.86 | 134 | empty |
| 2 | 1060 | 0.85 | 0.85 | 121 | empty |
| 3 | 1085 | 0.83 | 0.84 | 107 | empty |
| 4 | 838 | 0.83 | 0.85 | 86 | empty |
| 5 | 921 | 0.83 | 0.84 | 93 | empty |
Interfaces
53 interfaces between chains.
- T–U · 551 Ų buried · 4 hydrogen bonds · protein-protein
- K–L · 542 Ų buried · 1 hydrogen bond · protein-protein
- E–F · 531 Ų buried · 1 hydrogen bond · protein-protein
- G–H · 523 Ų buried · 2 hydrogen bonds · protein-protein
- F–H · 517 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 3QIL · Crystal structure analysis of the clathrin trimerization domain · the same entry in another collection · chain K against K, 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 P49951
- Elsewhere: RCSB PDB 3QIL · PDBe 3QIL · UniProt P49951
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