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Structure and dynamics of ferrocytochrome C553 from desulfovibrio vulgaris studied by NMR spectroscopy and restrained molecular dynamics

Analyse Structure and dynamics of ferrocytochrome C553 from desulfovibrio vulgaris… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1DVH
Type
protein
Length
79 residues
Chains
1
Method
solution nmr
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Cytochrome C553
UniProt
P04032
Ligands
HEC
Pockets
1 · best druggability 0.69

Structure

solution nmr · 1 distinct chain · 54% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACytochrome C553protein7954% helix, 0% strandP04032

Ligands and binding sites

  • HEC · Heme C · ligand · chains A

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.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12360.690.8531HEC

Modifications

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

Compared structures

  • 1DVH · Structure and dynamics of ferrocytochrome C553 from desulfovibrio vulgaris studied by NMR… · the same entry in another collection · chain A against A, TM-score 1.00
  • P04032 · AlphaFold monomer V2.0 prediction for cytochrome C-553 (P04032) · a predicted model of the same protein · chain A against A, TM-score 0.95
  • 1DWL · The Ferredoxin-Cytochrome complex using heteronuclear NMR and docking simulation · a predicted model of the same protein · chain A against B, TM-score 0.70
  • 1DWL · The ferredoxin-cytochrome complex using heteronuclear NMR and docking simulation · a predicted model of the same protein · chain A against B, TM-score 0.70

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