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Crystal structure of the cota native enzyme
Analyse Crystal structure of the cota native enzyme in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4Q89
- Type
- protein
- Length
- 1,000 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Spore coat protein a
- UniProt
- P07788
- Ligands
- CU, CL
- Pockets
- 11 · best druggability 0.73
Structure
x-ray diffraction · 2 distinct chains · 8% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Spore coat protein a | protein | 501 | 8% helix, 40% strand | P07788 |
| B | Spore coat protein a | protein | 499 | 8% helix, 41% strand | P07788 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1001 | 0.73 | 0.77 | 81 | empty |
| 2 | 144 | 0.54 | 0.81 | 30 | empty |
| 3 | 106 | 0.52 | 0.83 | 28 | empty |
| 4 | 120 | 0.47 | 0.79 | 29 | empty |
| 5 | 97 | 0.47 | 0.80 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 915 Ų buried · 18 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 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 4Q89 · PDBe 4Q89 · UniProt P07788
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