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Crystal structure of alkylhydroperoxide reductase subunit C from E. COLI

Analyse Crystal structure of alkylhydroperoxide reductase subunit C from E. COLI in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4O5R
Type
protein
Length
832 residues
Chains
5
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Ahpc component, subunit of alkylhydroperoxide reductase
EC
1.8.1.-, 1.11.1.15
UniProt
C6EK89
Pockets
15 · best druggability 0.73

Structure

x-ray diffraction · 3 distinct chains · 31% helix, 29% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, C, DAhpc component, subunit of alkylhydroperoxide reductase (EC 1.8.1.-, 1.11.1.15)protein16729% helix, 29% strandC6EK89
BAhpc component, subunit of alkylhydroperoxide reductase (EC 1.8.1.-, 1.11.1.15)protein16630% helix, 28% strandC6EK89
EAhpc component, subunit of alkylhydroperoxide reductase (EC 1.8.1.-, 1.11.1.15)protein16533% helix, 29% strandC6EK89

Pockets

15 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11250.730.9222empty
21220.730.9219empty
31630.540.8033empty
41490.540.8131empty
5910.520.8320empty

Interfaces

4 interfaces between chains.

  • C–D · 1318 Ų buried · 13 hydrogen bonds · protein-protein
  • A–B · 1252 Ų buried · 19 hydrogen bonds · protein-protein
  • B–C · 681 Ų buried · 0 hydrogen bonds · protein-protein
  • D–E · 671 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

  • 4O5R · Crystal structure of Alkylhydroperoxide Reductase subunit C from E. coli · the same entry in another collection · chain A against A, TM-score 1.00

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