MolNFT v1 · #80489 · protein
Crystal structure of oxo-cupper clusters binding to ferric binding protein from neisseria gonorrhoeae
3TYH · Fbpa protein: “Crystal structure of oxo-cupper clusters binding to ferric binding protein from neisseria gonorrhoeae”. X-ray diffraction, 1 ligand (CU), 20 pockets (best druggability 0.74). MolNFT v1 #80489 on GenesisL1: 3D…
- PDB
- 3TYH
- Type
- protein
- Length
- 2,781 residues
- Chains
- 9
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fbpa protein
- UniProt
- Q50964
- Ligands
- CU
- Pockets
- 20 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 46% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I | Fbpa protein | protein | 309 | 46% helix, 17% strand | Q50964 |
Ligands and binding sites
- CU · Copper (II) ion · metal · 18 copies · chains A, B, C, D, E, F, G, H, I
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 941 | 0.74 | 0.78 | 71 | CU |
| 2 | 1189 | 0.72 | 0.75 | 106 | CU |
| 3 | 425 | 0.68 | 0.80 | 56 | CU |
| 4 | 461 | 0.67 | 0.79 | 71 | CU |
| 5 | 265 | 0.64 | 0.82 | 44 | empty |
Interfaces
12 interfaces between chains.
- A–I · 357 Ų buried · 3 hydrogen bonds · protein-protein
- B–G · 320 Ų buried · 4 hydrogen bonds · protein-protein
- F–I · 312 Ų buried · 3 hydrogen bonds · protein-protein
- A–H · 280 Ų buried · 2 hydrogen bonds · protein-protein
- F–G · 230 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 3TYH · Crystal structure of oxo-cupper clusters binding to ferric binding protein from Neisseria… · 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 Q50964
- Elsewhere: RCSB PDB 3TYH · PDBe 3TYH · UniProt Q50964
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