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Heme-packing motifs revealed by the crystal structure of cytochrome C554 from nitrosomonas europaea

Analyse Heme-packing motifs revealed by the crystal structure of cytochrome C554 from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1BVB
Type
protein
Length
211 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Cytochrome C-554
UniProt
Q57142
Ligands
HEM, PO4
Pockets
1 · best druggability 0.85

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 4% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACytochrome C-554protein21135% helix, 4% strandQ57142

Ligands and binding sites

  • HEM · Protoporphyrin IX containing Fe · ligand · 4 copies · chains A
  • PO4 · Phosphate ion · ion · 3 copies · 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
111700.850.86102HEM

Modifications

Observed in the structure: 8 cofactor (heme attachment).

Compared structures

  • 1BVB · Heme-packing motifs revealed by the crystal structure of cytochrome C554 from… · the same entry in another collection · chain A against A, TM-score 1.00
  • Q57142 · AlphaFold monomer V2.0 prediction for cytochrome C-554 (Q57142) · a predicted model of the same protein · chain A against A, TM-score 0.98

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