GL1X · GenesisL1 explorer

Research workbench

Crystal structure of a complement factor H-binding fragment within the B75KN region of the group B streptococcus beta antigen C protein

Analyse Crystal structure of a complement factor H-binding fragment within the B75KN… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7S0R
Type
protein
Length
167 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
C protein beta antigen
UniProt
Q3MUG3
Pockets
1 · best druggability 0.34

Structure

x-ray diffraction · 2 distinct chains · 77% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AC protein beta antigenprotein8576% helix, 0% strandQ3MUG3
BC protein beta antigenprotein8278% helix, 0% strandQ3MUG3

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1840.340.7417empty

Interfaces

1 interface between chains.

  • A–B · 888 Ų buried · 13 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 modified (engineered).

Compared structures

  • 7S0R · Crystal Structure of a Complement Factor H-binding Fragment within the B75KN Region of… · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.