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Crystal structure of complement factor D mutant R202A after conventional refinement

Analyse Crystal structure of complement factor D mutant R202A after conventional… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4CBN
Type
protein
Length
456 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Complement factor D
EC
3.4.21.46
UniProt
P00746
Pockets
4 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 8% helix, 36% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BComplement factor D (EC 3.4.21.46)protein2288% helix, 36% strandP00746

Ligands and binding sites

  • GOL · Glycerol · additive · 3 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16630.690.7757empty
21420.510.8033empty
3870.350.7517empty
4720.330.7522empty

Interfaces

1 interface between chains.

  • A–B · 479 Ų buried · 5 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 disulfide (disulfide).

Compared structures

  • 4CBN · Crystal structure of Complement Factor D mutant R202A after conventional refinement · the same entry in another collection · chain A against A, TM-score 1.00
  • P00746 · AlphaFold monomer V2.0 prediction for complement factor D (P00746) · a predicted model of the same protein · chain A against A, TM-score 0.99

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