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Crystal structure of anopheline anti-platelet protein with Fab antibody

Analyse Crystal structure of anopheline anti-platelet protein with Fab antibody in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4OKV
Type
protein
Length
996 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Heavy chain of 8H7 mab; Light chain of 8H7 mab; Anti-platelet aggregation protein
UniProt
Q7YT37
Pockets
13 · best druggability 0.67

Structure

x-ray diffraction · 5 distinct chains · 19% helix, 43% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AHeavy chain of 8H7 mabprotein2147% helix, 50% strand—
B, DLight chain of 8H7 mabprotein2186% helix, 52% strand—
CHeavy chain of 8H7 mabprotein21510% helix, 51% strand—
EAnti-platelet aggregation proteinprotein6577% helix, 0% strandQ7YT37
FAnti-platelet aggregation proteinprotein6674% helix, 0% strandQ7YT37

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18140.670.7570empty
27560.660.7561empty
3850.530.8517empty
4800.510.8421empty
5770.480.8324empty

Interfaces

7 interfaces between chains.

  • C–D · 1765 Ų buried · 20 hydrogen bonds · protein-protein
  • A–B · 1701 Ų buried · 19 hydrogen bonds · protein-protein
  • E–F · 994 Ų buried · 5 hydrogen bonds · protein-protein
  • A–F · 503 Ų buried · 9 hydrogen bonds · protein-protein
  • C–E · 476 Ų buried · 7 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 12 disulfide (disulfide).

Compared structures

  • 4OKV · Crystal structure of anopheline anti-platelet protein with Fab antibody · the same entry in another collection · chain A against A, TM-score 1.00

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