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The structure of the N-terminal domain of human clathrin heavy chain 1 (ntd) in complex with ES9
Analyse The structure of the N-terminal domain of human clathrin heavy chain 1 (ntd) in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6E4L
- Type
- protein
- Length
- 358 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Clathrin heavy chain 1
- UniProt
- Q00610
- Ligands
- HRS
- Pockets
- 6 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 9% helix, 51% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Clathrin heavy chain 1 | protein | 358 | 9% helix, 51% strand | Q00610 |
Ligands and binding sites
- HRS · 5-bromo-N-(4-nitrophenyl)thiophene-2-sulfonamide · ligand · chains A
- ACT · Acetate ion · additive · 3 copies · chains A
- DMS · Dimethyl sulfoxide · additive · 2 copies · chains A
- EDO · 1,2-ethanediol · additive · 2 copies · chains A
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 735 | 0.77 | 0.81 | 77 | DMS, GOL |
| 2 | 57 | 0.34 | 0.77 | 12 | empty |
| 3 | 52 | 0.32 | 0.77 | 11 | ACT |
| 4 | 57 | 0.32 | 0.76 | 17 | empty |
| 5 | 57 | 0.30 | 0.76 | 13 | DMS |
Compared structures
- 6E4L · The structure of the N-terminal domain of human clathrin heavy chain 1 (nTD) in complex… · the same entry in another collection · chain A against A, TM-score 1.00
- Q00610 · AlphaFold monomer V2.0 prediction for clathrin heavy chain 1 (Q00610) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 Q00610
- Elsewhere: RCSB PDB 6E4L · PDBe 6E4L · UniProt Q00610
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