Research workbench
Histoplasma capsulatum H88 Calcium Binding Protein 1 (Cbp1)
Analyse Histoplasma capsulatum H88 Calcium Binding Protein 1 (Cbp1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7R79
- Type
- protein
- Length
- 306 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.6
- Source
- Ajellomyces capsulatus
- Molecule
- Calcium-binding protein
- UniProt
- F0UVX7
- Pockets
- 3 · best druggability 0.52
Structure
x-ray diffraction · resolution 1.6 · 2 distinct chains · 59% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D | Calcium-binding protein | protein | 76 | 61% helix, 0% strand | F0UVX7 |
| B, C | Calcium-binding protein | protein | 77 | 57% helix, 0% strand | F0UVX7 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 137 | 0.52 | 0.80 | 25 | empty |
| 2 | 97 | 0.45 | 0.80 | 22 | empty |
| 3 | 68 | 0.32 | 0.75 | 12 | empty |
Interfaces
5 interfaces between chains.
- C–D · 1178 Ų buried · 2 hydrogen bonds · protein-protein
- A–B · 1148 Ų buried · 3 hydrogen bonds · protein-protein
- B–D · 400 Ų buried · 1 hydrogen bond · protein-protein
- A–D · 232 Ų buried · 3 hydrogen bonds · protein-protein
- B–C · 174 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 12 disulfide (disulfide).
Compared structures
- 7R79 · Histoplasma capsulatum H88 calcium binding protein 1 (CBP1) · 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 F0UVX7
- Elsewhere: RCSB PDB 7R79 · PDBe 7R79 · UniProt F0UVX7
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