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Human insulin in complex with the analytical antibody oxi-005 Fab

Analyse Human insulin in complex with the analytical antibody oxi-005 Fab in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6Z7Y
Type
protein
Length
943 residues
Chains
8
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Oxi-005 Fab light chain; Oxi-005 Fab heavy chain; Insulin
UniProt
P01308
Pockets
13 · best druggability 0.52

Structure

x-ray diffraction · 7 distinct chains · 9% helix, 48% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AOxi-005 Fab light chainprotein2135% helix, 51% strand—
BOxi-005 Fab heavy chainprotein2117% helix, 52% strand—
COxi-005 Fab light chainprotein2115% helix, 54% strand—
DOxi-005 Fab heavy chainprotein2099% helix, 53% strand—
E, GInsulinprotein2148% helix, 5% strandP01308
FInsulinprotein2931% helix, 3% strandP01308
HInsulinprotein2832% helix, 4% strandP01308

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11120.520.8221empty
2760.520.8524empty
31460.460.7727empty
41550.450.7627empty
51150.380.7417empty

Interfaces

13 interfaces between chains.

  • A–B · 1914 Ų buried · 18 hydrogen bonds · protein-protein
  • C–D · 1751 Ų buried · 16 hydrogen bonds · protein-protein
  • E–F · 745 Ų buried · 11 hydrogen bonds · protein-protein
  • G–H · 726 Ų buried · 11 hydrogen bonds · protein-protein
  • D–F · 410 Ų buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 14 disulfide (disulfide).

Compared structures

  • 6Z7Y · Human insulin in complex with the analytical antibody OXI-005 Fab · the same entry in another collection · chain A against A, TM-score 1.00

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