MolNFT v1 · #118984 · protein
Apo-CSP3 (copper storage protein 3) from bacillus subtilis
5FIG: “Apo-CSP3 (copper storage protein 3) from bacillus subtilis”. X-ray diffraction, 6 pockets (best druggability 0.83). MolNFT v1 #118984 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5FIG
- Type
- protein
- Length
- 588 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- CSP3
- Pockets
- 6 · best druggability 0.83
Structure
x-ray diffraction · 5 distinct chains · 83% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, E | CSP3 | protein | 100 | 82% helix, 0% strand | — |
| B | CSP3 | protein | 102 | 80% helix, 0% strand | — |
| C | CSP3 | protein | 93 | 86% helix, 0% strand | — |
| D | CSP3 | protein | 90 | 87% helix, 0% strand | — |
| F | CSP3 | protein | 103 | 81% helix, 0% strand | — |
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 288 | 0.83 | 0.94 | 37 | empty |
| 2 | 409 | 0.64 | 0.78 | 32 | empty |
| 3 | 53 | 0.51 | 0.87 | 15 | empty |
| 4 | 109 | 0.37 | 0.74 | 22 | empty |
| 5 | 52 | 0.28 | 0.75 | 10 | empty |
Interfaces
10 interfaces between chains.
- A–C · 827 Ų buried · 11 hydrogen bonds · protein-protein
- B–D · 802 Ų buried · 12 hydrogen bonds · protein-protein
- E–F · 772 Ų buried · 7 hydrogen bonds · protein-protein
- A–B · 739 Ų buried · 5 hydrogen bonds · protein-protein
- C–D · 552 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 5FIG · Apo-CSP3 (copper storage protein 3) from bacillus subtilis · 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
- Elsewhere: RCSB PDB 5FIG · PDBe 5FIG
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