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Crystal Structure of Selenomethionine PcoC, a Copper Resistance Protein from Escherichia coli

Analyse Crystal Structure of Selenomethionine PcoC, a Copper Resistance Protein from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1IX2
Type
protein
Length
205 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
1.55
Source
Escherichia coli
Molecule
PcoC copper resistance protein
UniProt
Q47454
Pockets
1 · best druggability 0.60

Structure

x-ray diffraction · resolution 1.55 · 2 distinct chains · 3% helix, 51% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APcoC copper resistance proteinprotein1023% helix, 51% strandQ47454
BPcoC copper resistance proteinprotein1033% helix, 50% strandQ47454

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15300.600.7449empty

Interfaces

1 interface between chains.

  • A–B · 392 Ų buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 10 modified (engineered).

Compared structures

  • 1IX2 · Crystal structure of selenomethionine pcoc, a copper resistance protein from escherichia… · the same entry in another collection · chain A against A, TM-score 1.00
  • Q47454 · AlphaFold monomer V2.0 prediction for copper resistance protein C (Q47454) · a predicted model of the same protein · chain B against A, TM-score 0.96

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