Research workbench
201PHI2-1 chimallin localized tetramer reconstruction
Analyse 201PHI2-1 chimallin localized tetramer reconstruction in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7SQR
- Type
- protein
- Length
- 2,216 residues
- Chains
- 12
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chimallin
- UniProt
- B3FIW8
- Pockets
- 20 · best druggability 0.83
Structure
electron microscopy · 3 distinct chains · 34% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D, G, J | Chimallin | protein | 522 | 36% helix, 23% strand | B3FIW8 |
| B, E, H, K | Chimallin | protein | 22 | 14% helix, 0% strand | B3FIW8 |
| C, F, I, L | Chimallin | protein | 10 | 0% helix, 0% strand | B3FIW8 |
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 | 952 | 0.83 | 0.85 | 91 | empty |
| 2 | 1152 | 0.81 | 0.82 | 125 | empty |
| 3 | 1133 | 0.81 | 0.82 | 102 | empty |
| 4 | 1144 | 0.81 | 0.82 | 97 | empty |
| 5 | 1133 | 0.81 | 0.82 | 98 | empty |
Interfaces
12 interfaces between chains.
- G–J · 1310 Ų buried · 14 hydrogen bonds · protein-protein
- A–J · 1310 Ų buried · 14 hydrogen bonds · protein-protein
- D–G · 1309 Ų buried · 14 hydrogen bonds · protein-protein
- A–D · 1304 Ų buried · 14 hydrogen bonds · protein-protein
- A–B · 1220 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 7SQR · 201phi2-1 Chimallin localized tetramer 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 B3FIW8
- Elsewhere: RCSB PDB 7SQR · PDBe 7SQR · UniProt B3FIW8
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