Research workbench
Crystal structure of ctx A4 from taiwan cobra (naja naja atra)
Analyse Crystal structure of ctx A4 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
- 4OM5
- Type
- protein
- Length
- 240 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytotoxin 4
- UniProt
- P01443
- Pockets
- 4 · best druggability 0.45
Structure
x-ray diffraction · 1 distinct chain · 0% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Cytotoxin 4 | protein | 60 | 0% helix, 42% strand | P01443 |
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 76 | 0.45 | 0.81 | 18 | empty |
| 2 | 115 | 0.41 | 0.75 | 24 | empty |
| 3 | 67 | 0.37 | 0.77 | 14 | empty |
| 4 | 50 | 0.24 | 0.72 | 14 | empty |
Interfaces
4 interfaces between chains.
- A–C · 389 Ų buried · 4 hydrogen bonds · protein-protein
- A–B · 377 Ų buried · 0 hydrogen bonds · protein-protein
- B–D · 152 Ų buried · 0 hydrogen bonds · protein-protein
- A–D · 92 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 16 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 P01443
- Elsewhere: RCSB PDB 4OM5 · PDBe 4OM5 · UniProt P01443
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