Research workbench
Goslar chimallin C4 tetramer localized reconstruction
Analyse Goslar chimallin C4 tetramer localized reconstruction in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7SQU
- Type
- protein
- Length
- 2,292 residues
- Chains
- 12
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chimallin
- UniProt
- A0A482GDX1
- Pockets
- 20 · best druggability 0.81
Structure
electron microscopy · 3 distinct chains · 34% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D, G, J | Chimallin | protein | 542 | 35% helix, 26% strand | A0A482GDX1 |
| B, E, H, K | Chimallin | protein | 25 | 28% helix, 8% strand | A0A482GDX1 |
| C, F, I, L | Chimallin | protein | 6 | 0% helix, 0% strand | A0A482GDX1 |
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 | 449 | 0.81 | 0.88 | 51 | empty |
| 2 | 444 | 0.80 | 0.88 | 53 | empty |
| 3 | 453 | 0.80 | 0.87 | 54 | empty |
| 4 | 438 | 0.79 | 0.87 | 54 | empty |
| 5 | 935 | 0.78 | 0.81 | 96 | empty |
Interfaces
16 interfaces between chains.
- A–D · 1958 Ų buried · 21 hydrogen bonds · protein-protein
- G–J · 1955 Ų buried · 21 hydrogen bonds · protein-protein
- A–J · 1953 Ų buried · 21 hydrogen bonds · protein-protein
- D–G · 1952 Ų buried · 21 hydrogen bonds · protein-protein
- J–K · 1282 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
- 7SQU · Goslar chimallin C4 tetramer localized reconstruction · the same entry in another collection · chain A against A, 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 A0A482GDX1
- Elsewhere: RCSB PDB 7SQU · PDBe 7SQU · UniProt A0A482GDX1
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