MolNFT v1 · #154090 · protein
Crystal structure of sufu from bacillus subtilis
6JZV · Zinc-dependent sulfurtransferase sufu: “Crystal structure of sufu from bacillus subtilis”. X-ray diffraction, 1 ligand (ZN), 9 pockets (best druggability 0.72). MolNFT v1 #154090 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 6JZV
- Type
- protein
- Length
- 557 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Zinc-dependent sulfurtransferase sufu
- EC
- 2.-.-.-
- UniProt
- O32163
- Ligands
- ZN
- Pockets
- 9 · best druggability 0.72
Structure
x-ray diffraction · 4 distinct chains · 54% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Zinc-dependent sulfurtransferase sufu (EC 2.-.-.-) | protein | 141 | 53% helix, 21% strand | O32163 |
| B | Zinc-dependent sulfurtransferase sufu (EC 2.-.-.-) | protein | 141 | 54% helix, 21% strand | O32163 |
| C | Zinc-dependent sulfurtransferase sufu (EC 2.-.-.-) | protein | 139 | 54% helix, 22% strand | O32163 |
| D | Zinc-dependent sulfurtransferase sufu (EC 2.-.-.-) | protein | 136 | 56% helix, 22% strand | O32163 |
Ligands and binding sites
- ZN · Zinc ion · metal · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 646 | 0.72 | 0.79 | 53 | empty |
| 2 | 410 | 0.64 | 0.78 | 37 | empty |
| 3 | 300 | 0.62 | 0.79 | 36 | empty |
| 4 | 97 | 0.37 | 0.75 | 14 | empty |
| 5 | 81 | 0.36 | 0.76 | 14 | empty |
Interfaces
5 interfaces between chains.
- C–D · 499 Ų buried · 15 hydrogen bonds · protein-protein
- A–B · 495 Ų buried · 14 hydrogen bonds · protein-protein
- A–D · 439 Ų buried · 6 hydrogen bonds · protein-protein
- B–D · 292 Ų buried · 11 hydrogen bonds · protein-protein
- A–C · 253 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
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 O32163
- Elsewhere: RCSB PDB 6JZV · PDBe 6JZV · UniProt O32163
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