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Crystal structure of anti-upar Fab 8B12

Analyse Crystal structure of anti-upar Fab 8B12 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4QTH
Type
protein
Length
864 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Anti-upar antibody, heavy chain; Anti-upar antibody, light chain
Pockets
6 · best druggability 0.58

Structure

x-ray diffraction · 4 distinct chains · 7% helix, 51% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
HAnti-upar antibody, heavy chainprotein2249% helix, 51% strand—
LAnti-upar antibody, light chainprotein2146% helix, 51% strand—
AAnti-upar antibody, heavy chainprotein2156% helix, 52% strand—
BAnti-upar antibody, light chainprotein2117% helix, 52% strand—

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14530.580.7470empty
24720.570.7348empty
31120.520.8221empty
43020.520.7447empty
5530.350.7915empty

Interfaces

3 interfaces between chains.

  • H–L · 1887 Ų buried · 19 hydrogen bonds · protein-protein
  • A–B · 1670 Ų buried · 16 hydrogen bonds · protein-protein
  • H–B · 402 Ų buried · 9 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 9 disulfide (disulfide).

Compared structures

  • 4QTH · Crystal structure of anti-uPAR Fab 8B12 · the same entry in another collection · chain H against H, TM-score 1.00

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