Research workbench
The de novo evolutionary emergence of a symmetrical protein is shaped by folding constraints
Analyse The de novo evolutionary emergence of a symmetrical protein is shaped by… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5C2M
- Type
- protein
- Length
- 237 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Predicted protein
- UniProt
- A7SDD2
- Pockets
- 1 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 14% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Predicted protein | protein | 237 | 14% helix, 37% strand | A7SDD2 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 354 | 0.75 | 0.85 | 36 | empty |
Compared structures
- 5C2M · The de novo evolutionary emergence of a symmetrical protein is shaped by folding… · 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 A7SDD2
- Elsewhere: RCSB PDB 5C2M · PDBe 5C2M · UniProt A7SDD2
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