Research workbench
N-terminal beta-strand swapping in a consensus derived alternative scaffold driven by stabilizing hydrophobic interactions
Analyse N-terminal beta-strand swapping in a consensus derived alternative scaffold… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4M6A
- Type
- protein
- Length
- 883 residues
- Chains
- 10
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tencon
- Pockets
- 14 · best druggability 0.70
Structure
x-ray diffraction · 8 distinct chains · 0% helix, 57% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tencon | protein | 87 | 0% helix, 59% strand | — |
| B | Tencon | protein | 91 | 0% helix, 56% strand | — |
| C | Tencon | protein | 90 | 0% helix, 56% strand | — |
| D | Tencon | protein | 88 | 0% helix, 57% strand | — |
| E, F, H | Tencon | protein | 89 | 0% helix, 55% strand | — |
| G | Tencon | protein | 87 | 0% helix, 60% strand | — |
| I | Tencon | protein | 83 | 0% helix, 59% strand | — |
| J | Tencon | protein | 90 | 0% helix, 52% strand | — |
Pockets
14 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 708 | 0.70 | 0.77 | 92 | empty |
| 2 | 460 | 0.66 | 0.78 | 51 | empty |
| 3 | 416 | 0.58 | 0.75 | 47 | empty |
| 4 | 99 | 0.53 | 0.83 | 20 | empty |
| 5 | 147 | 0.48 | 0.77 | 19 | empty |
Interfaces
21 interfaces between chains.
- G–H · 2193 Ų buried · 49 hydrogen bonds · protein-protein
- C–D · 2185 Ų buried · 45 hydrogen bonds · protein-protein
- I–J · 2161 Ų buried · 40 hydrogen bonds · protein-protein
- A–B · 2151 Ų buried · 37 hydrogen bonds · protein-protein
- E–F · 2133 Ų buried · 35 hydrogen bonds · protein-protein
Compared structures
- 4M6A · N-Terminal beta-Strand Swapping in a Consensus Derived Alternative Scaffold Driven by… · the same entry in another collection · chain E against E, 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
- Elsewhere: RCSB PDB 4M6A · PDBe 4M6A
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