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Crystal structure of human Fab S24-1379 in the complex with the N- teminal domain of nucleocapsid protein from SARS cov-2

Analyse Crystal structure of human Fab S24-1379 in the complex with the N- teminal… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7STS
Type
protein
Length
1,074 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Fab S24-1379, heavy chain; Fab S24-1379, light chain; Nucleoprotein
UniProt
P0DTC9
Pockets
10 · best druggability 0.80

Structure

x-ray diffraction · 5 distinct chains · 4% helix, 44% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AFab S24-1379, heavy chainprotein2043% helix, 54% strand—
B, LFab S24-1379, light chainprotein2127% helix, 50% strand—
CNucleoproteinprotein1113% helix, 21% strandP0DTC9
DNucleoproteinprotein1250% helix, 24% strandP0DTC9
HFab S24-1379, heavy chainprotein2104% helix, 52% strand—

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19900.800.82111empty
24880.590.7458empty
34470.570.7444empty
41350.530.8022empty
5820.410.7919empty

Interfaces

10 interfaces between chains.

  • H–L · 1718 Ų buried · 13 hydrogen bonds · protein-protein
  • A–B · 1654 Ų buried · 13 hydrogen bonds · protein-protein
  • C–D · 541 Ų buried · 16 hydrogen bonds · protein-protein
  • C–H · 283 Ų buried · 2 hydrogen bonds · protein-protein
  • A–D · 282 Ų buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 disulfide (disulfide).

Compared structures

  • 7STS · Crystal Structure of Human Fab S24-1379 in the Complex with the N-teminal Domain of… · the same entry in another collection · chain A against A, TM-score 1.00

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