Research workbench
Crystal structure of ctx A2 from taiwan cobra (naja naja atra)
Analyse Crystal structure of ctx A2 from taiwan cobra (naja naja atra) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4OM4
- Type
- protein
- Length
- 300 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytotoxin 2
- UniProt
- P01442
- Pockets
- 3 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 0% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E | Cytotoxin 2 | protein | 60 | 0% helix, 40% strand | P01442 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 857 | 0.71 | 0.76 | 75 | empty |
| 2 | 113 | 0.43 | 0.77 | 22 | empty |
| 3 | 77 | 0.31 | 0.73 | 17 | empty |
Interfaces
6 interfaces between chains.
- A–B · 375 Ų buried · 5 hydrogen bonds · protein-protein
- A–C · 278 Ų buried · 0 hydrogen bonds · protein-protein
- C–E · 223 Ų buried · 0 hydrogen bonds · protein-protein
- A–D · 203 Ų buried · 2 hydrogen bonds · protein-protein
- A–E · 195 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 20 disulfide (disulfide).
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 P01442
- Elsewhere: RCSB PDB 4OM4 · PDBe 4OM4 · UniProt P01442
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