Research workbench
3D structure of cota incubated with sodium azide
Analyse 3D structure of cota incubated with sodium azide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1W6W
- Type
- protein
- Length
- 502 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Spore coat protein a
- UniProt
- P07788
- Ligands
- CU, AZI
- Pockets
- 7 · best druggability 0.55
Structure
x-ray diffraction · 1 distinct chain · 9% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Spore coat protein a | protein | 502 | 9% helix, 41% strand | P07788 |
Ligands and binding sites
- CU · Copper (II) ion · metal · 4 copies · chains A
- AZI · Azide ion · ion · chains A
- GOL · Glycerol · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 196 | 0.55 | 0.79 | 47 | empty |
| 2 | 153 | 0.55 | 0.81 | 31 | empty |
| 3 | 58 | 0.44 | 0.83 | 16 | empty |
| 4 | 99 | 0.34 | 0.73 | 21 | empty |
| 5 | 52 | 0.31 | 0.77 | 16 | empty |
Modifications
Observed in the structure: 1 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 P07788
- Elsewhere: RCSB PDB 1W6W · PDBe 1W6W · UniProt P07788
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