MolNFT v1 · #92296 · protein
Mutational analysis of sulfite reductase hemoprotein reveals the mechanism for coordinated electron and proton transfer
4G38 · Sulfite reductase [NADPH] hemoprotein beta-component: “Mutational analysis of sulfite reductase hemoprotein reveals the mechanism for coordinated electron and…”. X-ray diffraction, 4 ligands (SF4, SRM, K), 4 pockets (best…
- PDB
- 4G38
- Type
- protein
- Length
- 449 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
- 4 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Sulfite reductase [NADPH] hemoprotein beta-component (EC 1.8.1.2) | protein | 449 | 35% helix, 23% strand | P17846 |
Ligands and binding sites
- SF4 · Iron/sulfur cluster · ligand · chains A
- SRM · Siroheme · ligand · chains A
- K · Potassium ion · metal · chains A
- PO4 · Phosphate ion · ion · 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 438 | 0.74 | 0.83 | 52 | PO4, SF4, SRM |
| 2 | 81 | 0.39 | 0.77 | 16 | empty |
| 3 | 105 | 0.37 | 0.75 | 20 | empty |
| 4 | 66 | 0.32 | 0.76 | 18 | empty |
Compared structures
- 4G38 · 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 0.99
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 4G38 · PDBe 4G38 · UniProt P17846
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