MolNFT v1 · #26469 · protein
Neutron crystal structure of dissimilatory sulfite reductase D (dsrd)
1WQ2 · Protein dsvd: “Neutron crystal structure of dissimilatory sulfite reductase D (dsrd)”. Neutron diffraction, 1 ligand (SO4), 1 pocket (best druggability 0.30). MolNFT v1 #26469 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 1WQ2
- Type
- protein
- Length
- 131 residues
- Chains
- 2
- Method
- neutron diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein dsvd
- UniProt
- Q46582
- Ligands
- SO4
- Pockets
- 1 · best druggability 0.30
Structure
neutron diffraction · 2 distinct chains · 44% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein dsvd | protein | 65 | 43% helix, 22% strand | Q46582 |
| B | Protein dsvd | protein | 66 | 45% helix, 21% strand | Q46582 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 66 | 0.30 | 0.74 | 25 | empty |
Interfaces
1 interface between chains.
- A–B · 452 Ų buried · 6 hydrogen bonds · 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 Q46582
- Elsewhere: RCSB PDB 1WQ2 · PDBe 1WQ2 · UniProt Q46582
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