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Crystal structure of efb-C (N138A) / C3D complex

Analyse Crystal structure of efb-C (N138A) / C3D complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3D5R
Type
protein
Length
724 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Complement C3; Fibrinogen-binding protein
UniProt
P01024, A6QG59
Pockets
9 · best druggability 0.84

Structure

x-ray diffraction · 2 distinct chains · 68% helix, 2% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BComplement C3protein29764% helix, 2% strandP01024
C, DFibrinogen-binding proteinprotein6585% helix, 0% strandA6QG59

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12310.840.9745empty
22800.580.7729empty
32930.570.7734empty
4810.570.8720empty
52590.560.7729empty

Interfaces

3 interfaces between chains.

  • B–D · 906 Ų buried · 3 hydrogen bonds · protein-protein
  • A–C · 899 Ų buried · 3 hydrogen bonds · protein-protein
  • A–B · 659 Ų buried · 7 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

  • 3D5R · Crystal Structure of Efb-C (N138A) / C3d Complex · the same entry in another collection · chain D against D, TM-score 1.00
  • A6QG59 · AlphaFold monomer V2.0 prediction for fibrinogen-binding protein (A6QG59) · a predicted model of the same protein · chain C against A, TM-score 0.96
  • P01024 · AlphaFold monomer V2.0 prediction for complement C3 (P01024) · a predicted model of the same protein · chain A against A, TM-score 0.90

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