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Structural basis for host specificity of factor H binding by streptococcus pneumoniae

Analyse Structural basis for host specificity of factor H binding by streptococcus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4K12
Type
protein
Length
146 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Complement factor H; Choline binding protein a
UniProt
P08603, G6W2B2
Pockets
1 · best druggability 0.56

Structure

x-ray diffraction · 2 distinct chains · 49% helix, 20% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AComplement factor Hprotein645% helix, 45% strandP08603
BCholine binding protein aprotein8283% helix, 0% strandG6W2B2

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11680.560.8125empty

Interfaces

1 interface between chains.

  • A–B · 686 Ų buried · 7 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

  • 4K12 · Structural Basis for Host Specificity of Factor H Binding by Streptococcus pneumoniae · the same entry in another collection · chain A against A, TM-score 1.00
  • P08603 · AlphaFold monomer V2.0 prediction for complement factor H (P08603) · a predicted model of the same protein · chain A against A, TM-score 0.91

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