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Crystallographic structure of the C24 protein from the antarctic microorganism bizionia argentinensis
Analyse Crystallographic structure of the C24 protein from the antarctic microorganism… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6OV6
- Type
- protein
- Length
- 739 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- C24 protein
- UniProt
- G2EBB4
- Ligands
- MN
- Pockets
- 4 · best druggability 0.85
Structure
x-ray diffraction · 3 distinct chains · 10% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | C24 protein | protein | 255 | 10% helix, 38% strand | G2EBB4 |
| B | C24 protein | protein | 240 | 10% helix, 35% strand | G2EBB4 |
| C | C24 protein | protein | 244 | 9% helix, 36% strand | G2EBB4 |
Ligands and binding sites
- MN · Manganese (II) ion · metal · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 302 | 0.85 | 0.96 | 39 | empty |
| 2 | 74 | 0.75 | 0.98 | 28 | empty |
| 3 | 183 | 0.46 | 0.75 | 20 | empty |
| 4 | 114 | 0.40 | 0.75 | 18 | empty |
Interfaces
3 interfaces between chains.
- A–B · 5124 Ų buried · 103 hydrogen bonds · protein-protein
- A–C · 5097 Ų buried · 97 hydrogen bonds · protein-protein
- B–C · 5041 Ų buried · 108 hydrogen bonds · protein-protein
Compared structures
- 6OV6 · Crystallographic structure of the C24 protein from the antarctic microorganism bizionia… · the same entry in another collection · chain A against A, TM-score 1.00
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 G2EBB4
- Elsewhere: RCSB PDB 6OV6 · PDBe 6OV6 · UniProt G2EBB4
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