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Structure of a complex between neisseria meningitidis factor H binding protein and ccps 6-7 of human complement factor H

Analyse Structure of a complex between neisseria meningitidis factor H binding protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2W80
Type
protein
Length
1,467 residues
Chains
8
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Complement factor H; Factor H binding protein
UniProt
P08603, Q9JXV4
Pockets
19 · best druggability 0.69

Structure

x-ray diffraction · 3 distinct chains · 6% helix, 57% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, E, GComplement factor Hprotein1238% helix, 37% strandP08603
CFactor H binding proteinprotein2435% helix, 63% strandQ9JXV4
D, F, HFactor H binding proteinprotein2446% helix, 61% strandQ9JXV4

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1590.690.9618empty
2550.670.9621empty
3560.660.9518empty
4540.650.9520empty
54770.600.7464empty

Interfaces

9 interfaces between chains.

  • E–F · 1630 Ų buried · 29 hydrogen bonds · protein-protein
  • B–C · 1624 Ų buried · 28 hydrogen bonds · protein-protein
  • A–D · 1621 Ų buried · 36 hydrogen bonds · protein-protein
  • G–H · 1576 Ų buried · 32 hydrogen bonds · protein-protein
  • C–F · 200 Ų buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 16 disulfide (disulfide).

Compared structures

  • 2W80 · Structure of a complex between Neisseria meningitidis factor H binding protein and CCPs… · the same entry in another collection · chain H against H, TM-score 1.00
  • P08603 · AlphaFold monomer V2.0 prediction for complement factor H (P08603) · a predicted model of the same protein · chain B against A, TM-score 0.64

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