Research workbench
Three-dimensional crystal structure of dissimilatory sulfite reductase D (dsrd)
Analyse Three-dimensional crystal structure of dissimilatory sulfite reductase D (dsrd) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1UCR
- Type
- protein
- Length
- 149 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein dsvd
- UniProt
- Q46582
- Ligands
- SO4
- Pockets
- 1 · best druggability 0.62
Structure
x-ray diffraction · 2 distinct chains · 52% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein dsvd | protein | 74 | 54% helix, 19% strand | Q46582 |
| B | Protein dsvd | protein | 75 | 49% helix, 19% strand | Q46582 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 5 copies · chains A, 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 145 | 0.62 | 0.86 | 38 | empty |
Interfaces
1 interface between chains.
- A–B · 926 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 1UCR · Three-dimensional crystal structure of dissimilatory sulfite reductase D (DsrD) · the same entry in another collection · chain A against A, TM-score 1.00
- Q46582 · AlphaFold monomer V2.0 prediction for protein dsvd (Q46582) · a predicted model of the same protein · chain B against A, TM-score 0.86
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 1UCR · PDBe 1UCR · UniProt Q46582
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