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Complement component C4B

Analyse Complement component C4B in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4XAM
Type
protein
Length
3,128 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Complement C4 beta chain; Complement C4-a alpha chain; Complement C4 gamma chain
UniProt
P0C0L4
Pockets
20 · best druggability 0.82

Structure

x-ray diffraction · 3 distinct chains · 17% helix, 35% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BComplement C4 beta chainprotein6516% helix, 47% strandP0C0L4
C, EComplement C4-a alpha chainprotein63230% helix, 21% strandP0C0L4
D, FComplement C4 gamma chainprotein28111% helix, 38% strandP0C0L4

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12480.820.9452empty
22520.810.9352empty
3730.750.9830empty
4720.740.9729empty
5670.720.9720empty

Interfaces

9 interfaces between chains.

  • A–C · 5031 Ų buried · 83 hydrogen bonds · protein-protein
  • B–E · 4993 Ų buried · 74 hydrogen bonds · protein-protein
  • C–D · 2573 Ų buried · 35 hydrogen bonds · protein-protein
  • E–F · 2528 Ų buried · 34 hydrogen bonds · protein-protein
  • B–F · 821 Ų buried · 9 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 20 disulfide (disulfide).

Compared structures

  • P0C0L4 · AlphaFold monomer V2.0 prediction for complement C4-a (P0C0L4) · a predicted model of the same protein · chain B against A, TM-score 0.98

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