MolNFT v1 · #128742 · protein
The structure of the copi coat linkage II
5NZU · Coatomer subunit alpha: “The structure of the copi coat linkage II”. Electron microscopy, 20 pockets (best druggability 0.78). MolNFT v1 #128742 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5NZU
- Type
- protein
- Length
- 4,996 residues
- Chains
- 11
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Coatomer subunit alpha; Coatomer subunit beta; Coatomer subunit beta'; Coatomer subunit…
- UniProt
- Q8CIE6, Q9JIF7, O55029, Q5XJY5, P11076, Q9QZE5, P61924
- Pockets
- 20 · best druggability 0.78
Structure
electron microscopy · 8 distinct chains · 36% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Coatomer subunit alpha | protein | 813 | 15% helix, 27% strand | Q8CIE6 |
| B | Coatomer subunit beta | protein | 800 | 57% helix, 9% strand | Q9JIF7 |
| C | Coatomer subunit beta' | protein | 843 | 23% helix, 33% strand | O55029 |
| D | Coatomer subunit delta | protein | 427 | 26% helix, 39% strand | Q5XJY5 |
| F, R, M | ADP-ribosylation factor 1 | protein | 159 | 29% helix, 21% strand | P11076 |
| G | Coatomer subunit gamma-1 | protein | 798 | 53% helix, 14% strand | Q9QZE5 |
| Z, L | Coatomer subunit zeta-1 | protein | 139 | 40% helix, 19% strand | P61924 |
| K | Coatomer subunit gamma-1 | protein | 560 | 45% helix, 20% strand | Q9QZE5 |
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 | 1193 | 0.78 | 0.81 | 135 | empty |
| 2 | 879 | 0.74 | 0.79 | 107 | empty |
| 3 | 465 | 0.72 | 0.82 | 87 | empty |
| 4 | 446 | 0.69 | 0.81 | 60 | empty |
| 5 | 324 | 0.67 | 0.83 | 47 | empty |
Interfaces
11 interfaces between chains.
- A–C · 1044 Ų buried · 41 hydrogen bonds · protein-protein
- A–B · 182 Ų buried · 2 hydrogen bonds · protein-protein
- G–R · 131 Ų buried · 8 hydrogen bonds · protein-protein
- K–M · 123 Ų buried · 4 hydrogen bonds · protein-protein
- B–G · 97 Ų buried · 1 hydrogen bond · 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 Q8CIE6
- Every structure of UniProt Q9JIF7
- Every structure of UniProt O55029
- Every structure of UniProt Q5XJY5
- Every structure of UniProt P11076
- Every structure of UniProt Q9QZE5
- Every structure of UniProt P61924
- Elsewhere: RCSB PDB 5NZU · PDBe 5NZU · UniProt Q8CIE6 · UniProt Q9JIF7 · UniProt O55029 · UniProt Q5XJY5 · UniProt P11076 · UniProt Q9QZE5 · UniProt P61924
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