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Crystal structure of outer surface protein C (ospc)

Analyse Crystal structure of outer surface protein C (ospc) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1F1M
Type
protein
Length
648 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Outer surface protein C
UniProt
Q9AGB1
Ligands
ZN
Pockets
3 · best druggability 0.42

Structure

x-ray diffraction · 1 distinct chain · 67% helix, 2% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, DOuter surface protein Cprotein16267% helix, 2% strandQ9AGB1

Ligands and binding sites

  • ZN · Zinc ion · metal · 6 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, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11220.420.7621empty
2960.410.7722empty
31060.390.7517empty

Interfaces

2 interfaces between chains.

  • A–B · 2310 Ų buried · 14 hydrogen bonds · protein-protein
  • C–D · 2267 Ų buried · 14 hydrogen bonds · protein-protein

Compared structures

  • 1F1M · Crystal structure of outer surface protein C (ospc) · the same entry in another collection · chain A against A, TM-score 1.00

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