Research workbench
Sulfite reductase hemoprotein in complex with a partially oxidized sulfide species
Analyse Sulfite reductase hemoprotein in complex with a partially oxidized sulfide… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7GEP
- Type
- protein
- Length
- 469 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Sulfite reductase hemoprotein
- EC
- 1.8.1.2
- UniProt
- P17846
- Ligands
- SF4, SRM, SX, NA
- Pockets
- 4 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Sulfite reductase hemoprotein (EC 1.8.1.2) | protein | 469 | 35% helix, 22% strand | P17846 |
Ligands and binding sites
- SF4 · Iron/sulfur cluster · ligand · chains A
- SRM · Siroheme · ligand · chains A
- SX · Sulfur oxide · ligand · chains A
- NA · Sodium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 518 | 0.77 | 0.84 | 65 | SF4, SRM, SX |
| 2 | 77 | 0.50 | 0.84 | 29 | empty |
| 3 | 64 | 0.31 | 0.75 | 16 | empty |
| 4 | 58 | 0.29 | 0.74 | 15 | empty |
Compared structures
- 7GEP · Sulfite reductase hemoprotein in complex with a partially oxidized sulfide species · the same entry in another collection · chain A against A, TM-score 1.00
- P17846 · AlphaFold monomer V2.0 prediction for sulfite reductase [NADPH] hemoprotein… · a predicted model of the same protein · 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 P17846
- Elsewhere: RCSB PDB 7GEP · PDBe 7GEP · UniProt P17846
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