Research workbench
Mutational analysis of sulfite reductase hemoprotein reveals the mechanism for coordinated electron and proton transfer
Analyse Mutational analysis of sulfite reductase hemoprotein reveals the mechanism for… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4G39
- Type
- protein
- Length
- 465 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Sulfite reductase [NADPH] hemoprotein beta-component
- EC
- 1.8.1.2
- UniProt
- P17846
- Ligands
- SF4, SRM, K, PO4
- Pockets
- 3 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Sulfite reductase [NADPH] hemoprotein beta-component (EC 1.8.1.2) | protein | 465 | 35% helix, 24% strand | P17846 |
Ligands and binding sites
- SF4 · Iron/sulfur cluster · ligand · chains A
- SRM · Siroheme · ligand · chains A
- K · Potassium ion · metal · 2 copies · chains A
- PO4 · Phosphate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 505 | 0.78 | 0.85 | 59 | PO4, SF4, SRM |
| 2 | 106 | 0.43 | 0.78 | 23 | empty |
| 3 | 61 | 0.30 | 0.75 | 16 | K |
Compared structures
- 4G39 · Mutational analysis of sulfite reductase hemoprotein reveals the mechanism for… · 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 4G39 · PDBe 4G39 · UniProt P17846
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