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Crystal structure of bovine Fab E03

Analyse Crystal structure of bovine Fab E03 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5IJV
Type
protein
Length
1,842 residues
Chains
8
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Bovine Fab E03 light chain; Bovine Fab E03 heavy chain
Pockets
20 · best druggability 0.73

Structure

x-ray diffraction · 5 distinct chains · 5% helix, 54% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
L, A, C, EBovine Fab E03 light chainprotein2138% helix, 52% strand—
HBovine Fab E03 heavy chainprotein2465% helix, 56% strand—
BBovine Fab E03 heavy chainprotein2485% helix, 55% strand—
DBovine Fab E03 heavy chainprotein2474% helix, 55% strand—
FBovine Fab E03 heavy chainprotein2495% helix, 53% strand—

Pockets

20 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16540.730.8078empty
24540.680.8052empty
36420.660.7652empty
47590.640.7367empty
54080.620.7753empty

Interfaces

15 interfaces between chains.

  • A–B · 2085 Ų buried · 14 hydrogen bonds · protein-protein
  • E–F · 2079 Ų buried · 13 hydrogen bonds · protein-protein
  • L–H · 2057 Ų buried · 14 hydrogen bonds · protein-protein
  • C–D · 2055 Ų buried · 19 hydrogen bonds · protein-protein
  • H–B · 478 Ų buried · 12 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 27 disulfide (disulfide).

Compared structures

  • 5IJV · Crystal structure of bovine Fab E03 · the same entry in another collection · chain L against L, TM-score 1.00

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