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Structure of a llama glama Fab 48A2 against human cmet

Analyse Structure of a llama glama Fab 48A2 against human cmet in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4R96
Type
protein
Length
1,736 residues
Chains
8
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Llama glama Fab 48A2 against human cmet L chain; Llama glama Fab 48A2 against human cmet…
Pockets
20 · best druggability 0.78

Structure

x-ray diffraction · 4 distinct chains · 5% helix, 50% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, CLlama glama Fab 48A2 against human cmet L chainprotein2196% helix, 52% strand—
E, LLlama glama Fab 48A2 against human cmet L chainprotein2215% helix, 47% strand—
B, D, FLlama glama Fab 48A2 against human cmet H chainprotein2138% helix, 51% strand—
HLlama glama Fab 48A2 against human cmet H chainprotein2173% helix, 50% strand—

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110330.780.8086empty
28000.770.8192empty
32450.650.8340empty
45420.620.7563empty
51670.600.8429empty

Interfaces

13 interfaces between chains.

  • L–H · 1859 Ų buried · 12 hydrogen bonds · protein-protein
  • C–D · 1758 Ų buried · 10 hydrogen bonds · protein-protein
  • A–B · 1734 Ų buried · 12 hydrogen bonds · protein-protein
  • E–F · 1732 Ų buried · 12 hydrogen bonds · protein-protein
  • B–H · 567 Ų buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 16 disulfide (disulfide).

Compared structures

  • 4R96 · Structure of a Llama Glama Fab 48A2 against human cMet · the same entry in another collection · chain A against A, TM-score 1.00

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