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Crystal structure of N64DEL mutant of nitrosomonas europaea cytochrome C552 (monoclinic space group)

Analyse Crystal structure of N64DEL mutant of nitrosomonas europaea cytochrome C552… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3ZOX
Type
protein
Length
320 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Cytochrome C-552
EC
1.7.2.2
UniProt
P95339
Ligands
HEC
Pockets
3 · best druggability 0.84

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 3% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, DCytochrome C-552 (EC 1.7.2.2)protein8046% helix, 3% strandP95339

Ligands and binding sites

  • HEC · Heme C · ligand · 4 copies · chains A, B, C, D

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14940.840.9073HEC
28760.810.83103HEC
32230.760.9034HEC

Interfaces

5 interfaces between chains.

  • B–C · 547 Ų buried · 4 hydrogen bonds · protein-protein
  • A–D · 534 Ų buried · 4 hydrogen bonds · protein-protein
  • A–B · 319 Ų buried · 1 hydrogen bond · protein-protein
  • A–C · 215 Ų buried · 1 hydrogen bond · protein-protein
  • B–D · 202 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

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

Compared structures

  • 3ZOX · Crystal Structure of N64Del Mutant of Nitrosomonas europaea Cytochrome c552 (monoclinic… · the same entry in another collection · chain D against D, TM-score 1.00
  • P95339 · AlphaFold monomer V2.0 prediction for cytochrome C-552 (P95339) · a predicted model of the same protein · chain B against A, TM-score 0.98

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