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Crystal structure of MAD2-6 IgG Fab in complex with pfcsp N-terminal peptide.

Analyse Crystal structure of MAD2-6 IgG Fab in complex with pfcsp N-terminal peptide. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7K76
Type
protein
Length
876 residues
Chains
5
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Heavy chain of MAD2-6 IgG Fab; Light chain of MAD2-6 IgG Fab; Pfcsp N-terminal peptide P17
Pockets
7 · best druggability 0.78

Structure

x-ray diffraction · 5 distinct chains · 6% helix, 50% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AHeavy chain of MAD2-6 IgG Fabprotein2237% helix, 49% strand—
BLight chain of MAD2-6 IgG Fabprotein2126% helix, 51% strand—
HHeavy chain of MAD2-6 IgG Fabprotein2177% helix, 50% strand—
LLight chain of MAD2-6 IgG Fabprotein2136% helix, 51% strand—
PPfcsp N-terminal peptide P17protein110% helix, 18% strand—

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1940.780.9929empty
27550.670.7566empty
37650.650.7465empty
43040.550.7651empty
5540.490.8620empty

Interfaces

9 interfaces between chains.

  • A–B · 1822 Ų buried · 16 hydrogen bonds · protein-protein
  • H–L · 1682 Ų buried · 15 hydrogen bonds · protein-protein
  • A–L · 362 Ų buried · 7 hydrogen bonds · protein-protein
  • H–P · 301 Ų buried · 6 hydrogen bonds · protein-protein
  • B–P · 276 Ų buried · 7 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 disulfide (disulfide).

Compared structures

  • 7K76 · Crystal structure of MAD2-6 IgG Fab in complex with PfCSP N-terminal peptide. · the same entry in another collection · chain A against A, TM-score 1.00

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