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Crystal structure of the unmodified A.17 antibody Fab fragment - L47R mutant

Analyse Crystal structure of the unmodified A.17 antibody Fab fragment - L47R mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6Y1K
Type
protein
Length
432 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Fab A.17 L47R mutant heavy chain; Fab A.17 L47R mutant light chain
Pockets
4 · best druggability 0.65

Structure

x-ray diffraction · 2 distinct chains · 6% helix, 50% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
HFab A.17 L47R mutant heavy chainprotein2168% helix, 51% strand—
LFab A.17 L47R mutant light chainprotein2164% helix, 49% strand—

Pockets

4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12390.650.8339empty
25660.610.7470empty
3520.510.8821empty
41230.440.7727empty

Interfaces

1 interface between chains.

  • H–L · 1826 Ų buried · 24 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 5 disulfide (disulfide).

Compared structures

  • 6Y1K · Crystal structure of the unmodified A.17 antibody FAB fragment - L47R mutant · the same entry in another collection · chain H against H, TM-score 1.00

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