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CAT192 Fab wild type

Analyse CAT192 Fab wild type in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6AMJ
Type
protein
Length
837 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
CAT192 Fab light chain; CAT192 Fab heavy chain
Ligands
NA
Pockets
12 · best druggability 0.75

Structure

x-ray diffraction · 4 distinct chains · 6% helix, 51% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
LCAT192 Fab light chainprotein2115% helix, 50% strand—
ACAT192 Fab light chainprotein2146% helix, 50% strand—
HCAT192 Fab heavy chainprotein2056% helix, 54% strand—
BCAT192 Fab heavy chainprotein2076% helix, 50% strand—

Ligands and binding sites

  • NA · Sodium ion · metal · chains L, H
  • PEG · Di(hydroxyethyl)ether · additive · chains L, H

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18950.750.7990empty
25320.690.7963empty
33180.580.7638empty
42620.560.7729empty
52150.560.7924empty

Interfaces

5 interfaces between chains.

  • L–H · 1731 Ų buried · 13 hydrogen bonds · protein-protein
  • A–B · 1664 Ų buried · 11 hydrogen bonds · protein-protein
  • L–A · 1158 Ų buried · 15 hydrogen bonds · protein-protein
  • A–H · 63 Ų buried · 0 hydrogen bonds · protein-protein
  • L–B · 59 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 9 disulfide (disulfide).

Compared structures

  • 6AMJ · CAT192 Fab Wild Type · the same entry in another collection · chain B against B, TM-score 1.00

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