Research workbench
Apo structure of porcine CD38
Analyse Apo structure of porcine CD38 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5BNF
- Type
- protein
- Length
- 454 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Uncharacterized protein
- UniProt
- F1S5D9
- Pockets
- 5 · best druggability 0.77
Structure
x-ray diffraction · 2 distinct chains · 39% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Uncharacterized protein | protein | 222 | 39% helix, 14% strand | F1S5D9 |
| B | Uncharacterized protein | protein | 232 | 40% helix, 14% strand | F1S5D9 |
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 958 | 0.77 | 0.79 | 97 | empty |
| 2 | 62 | 0.65 | 0.93 | 16 | empty |
| 3 | 55 | 0.53 | 0.88 | 13 | empty |
| 4 | 67 | 0.33 | 0.76 | 21 | empty |
| 5 | 61 | 0.32 | 0.76 | 11 | empty |
Interfaces
1 interface between chains.
- A–B · 643 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 10 disulfide (disulfide).
Compared structures
- 5BNF · Apo structure of porcine CD38 · 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 F1S5D9
- Elsewhere: RCSB PDB 5BNF · PDBe 5BNF · UniProt F1S5D9
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