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Sulfite dehydrogenase from starkeya novella

Analyse Sulfite dehydrogenase from starkeya novella in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2BLF
Type
protein
Length
454 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
SULFITE:CYTOCHROME C oxidoreductase subunit a; SULFITE:CYTOCHROME C oxidoreductase…
UniProt
Q9LA16, Q9LA15
Ligands
MSS, HEC, SO4
Pockets
5 · best druggability 0.79

Structure

x-ray diffraction · 2 distinct chains · 17% helix, 32% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ASULFITE:CYTOCHROME C oxidoreductase subunit aprotein37311% helix, 38% strandQ9LA16
BSULFITE:CYTOCHROME C oxidoreductase subunit Bprotein8148% helix, 2% strandQ9LA15

Ligands and binding sites

  • MSS · (molybdopterin-S,S)-oxo-molybdenum · ligand · chains A
  • HEC · Heme C · ligand · chains A, B
  • SO4 · Sulfate ion · ion · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16110.790.8469HEC
2850.760.9822MSS
31850.500.7726empty
41380.450.7722empty
51080.450.7831empty

Interfaces

1 interface between chains.

  • A–B · 1383 Ų buried · 26 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 cofactor, 1 disulfide (heme c attachment, disulfide).

Compared structures

  • 2BLF · Sulfite dehydrogenase from Starkeya Novella · the same entry in another collection · chain A against A, TM-score 1.00

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