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Crystal structure of cota native enzyme, PH8.0
Analyse Crystal structure of cota native enzyme, PH8.0 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5ZLJ
- Type
- protein
- Length
- 503 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Spore coat protein a
- UniProt
- P07788
- Ligands
- CU
- Pockets
- 5 · best druggability 0.53
Structure
x-ray diffraction · 1 distinct chain · 8% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Spore coat protein a | protein | 503 | 8% helix, 41% strand | P07788 |
Ligands and binding sites
- CU · Copper (II) ion · metal · 4 copies · chains A
- EDO · 1,2-ethanediol · additive · 9 copies · chains A
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 168 | 0.53 | 0.80 | 32 | empty |
| 2 | 87 | 0.50 | 0.83 | 14 | empty |
| 3 | 117 | 0.49 | 0.80 | 26 | EDO |
| 4 | 98 | 0.34 | 0.74 | 21 | empty |
| 5 | 60 | 0.30 | 0.75 | 15 | 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 5ZLJ · PDBe 5ZLJ · UniProt P07788
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