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Crystal structure analysis of the germline antibody 36-65 Fab in complex with the dodecapeptide slgdnltnhnlr

Analyse Crystal structure analysis of the germline antibody 36-65 Fab in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2A6K
Type
protein
Length
872 residues
Chains
5
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Germline antibody 36-65 Fab light chain; Germline antibody 36-65 Fab heavy chain…
UniProt
Q6PF95
Pockets
5 · best druggability 0.49

Structure

x-ray diffraction · 4 distinct chains · 6% helix, 50% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, LGermline antibody 36-65 Fab light chainprotein2146% helix, 50% strand—
BGermline antibody 36-65 Fab heavy chainprotein2186% helix, 52% strandQ6PF95
HGermline antibody 36-65 Fab heavy chainprotein2166% helix, 50% strandQ6PF95
PDodecapeptide: slgdnltnhnlrprotein100% helix, 0% strand—

Pockets

5 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12310.490.7436empty
22460.480.7344empty
3730.300.7318empty
4680.290.7318empty
5680.260.7213empty

Interfaces

4 interfaces between chains.

  • A–B · 1968 Ų buried · 20 hydrogen bonds · protein-protein
  • L–H · 1904 Ų buried · 13 hydrogen bonds · protein-protein
  • H–P · 403 Ų buried · 11 hydrogen bonds · protein-protein
  • L–P · 98 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 disulfide (disulfide).

Compared structures

  • 2A6K · Crystal Structure Analysis of the germline antibody 36-65 Fab in complex with the… · the same entry in another collection · chain A against A, TM-score 1.00

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