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Crystal structure of human na-22 Fab

Analyse Crystal structure of human na-22 Fab in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6PZH
Type
protein
Length
872 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Na-22 Fab light chain; Na-22 Fab heavy chain
Pockets
7 · best druggability 0.67

Structure

x-ray diffraction · 3 distinct chains · 7% helix, 50% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
LNa-22 Fab light chainprotein2136% helix, 50% strand—
H, BNa-22 Fab heavy chainprotein2228% helix, 50% strand—
ANa-22 Fab light chainprotein2156% helix, 50% strand—

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16760.670.7666empty
25170.670.7874empty
34020.580.7541empty
43020.580.7751empty
51890.450.7526empty

Interfaces

5 interfaces between chains.

  • A–B · 1950 Ų buried · 13 hydrogen bonds · protein-protein
  • L–H · 1931 Ų buried · 9 hydrogen bonds · protein-protein
  • L–A · 109 Ų buried · 0 hydrogen bonds · protein-protein
  • H–A · 104 Ų buried · 0 hydrogen bonds · protein-protein
  • L–B · 73 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 10 disulfide (disulfide).

Compared structures

  • 6PZH · Crystal structure of human NA-22 Fab · the same entry in another collection · chain L against L, TM-score 1.00

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