MolNFT v1 · #129217 · protein
Structure of a phosphoprotein-protein complex
5ODS · Clathrin heavy chain 1: “Structure of a phosphoprotein-protein complex”. X-ray diffraction, 20 pockets (best druggability 0.78). MolNFT v1 #129217 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5ODS
- Type
- protein
- Length
- 2,336 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Clathrin heavy chain 1; Lys-glu-ser-ala-leu-arg-lys-gln-sep-leu-tyr-leu-lys-phe…
- UniProt
- Q68FD5
- Pockets
- 20 · best druggability 0.78
Structure
x-ray diffraction · 5 distinct chains · 31% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Clathrin heavy chain 1 | protein | 572 | 31% helix, 31% strand | Q68FD5 |
| B | Clathrin heavy chain 1 | protein | 567 | 30% helix, 32% strand | Q68FD5 |
| C | Clathrin heavy chain 1 | protein | 554 | 30% helix, 31% strand | Q68FD5 |
| D | Clathrin heavy chain 1 | protein | 571 | 30% helix, 31% strand | Q68FD5 |
| E, F, G, H | Lys-glu-ser-ala-leu-arg-lys-gln-sep-leu-tyr-leu-lys-phe- asp-pro-leu-leu | protein | 18 | 67% helix, 0% strand | — |
Pockets
20 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 575 | 0.78 | 0.84 | 60 | empty |
| 2 | 695 | 0.76 | 0.81 | 70 | empty |
| 3 | 674 | 0.75 | 0.81 | 69 | empty |
| 4 | 586 | 0.74 | 0.81 | 61 | empty |
| 5 | 567 | 0.74 | 0.81 | 63 | empty |
Interfaces
11 interfaces between chains.
- A–B · 1029 Ų buried · 16 hydrogen bonds · protein-protein
- D–H · 521 Ų buried · 4 hydrogen bonds · protein-protein
- B–F · 498 Ų buried · 1 hydrogen bond · protein-protein
- A–E · 483 Ų buried · 2 hydrogen bonds · protein-protein
- C–G · 444 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (phosphorylation).
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 Q68FD5
- Elsewhere: RCSB PDB 5ODS · PDBe 5ODS · UniProt Q68FD5
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