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Crystal structure of disulfide-bonded diabody

Analyse Crystal structure of disulfide-bonded diabody in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5GRX
Type
protein
Length
460 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Diabody protein
Pockets
3 · best druggability 0.46

Structure

x-ray diffraction · 2 distinct chains · 8% helix, 49% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
GDiabody proteinprotein2298% helix, 49% strand—
HDiabody proteinprotein2318% helix, 49% strand—

Pockets

3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11040.460.7920empty
21580.400.7329empty
31390.380.7319empty

Interfaces

1 interface between chains.

  • G–H · 2055 Ų buried · 29 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 5 disulfide (disulfide).

Compared structures

  • 5GRX · Crystal structure of disulfide-bonded diabody · the same entry in another collection · chain G against G, TM-score 1.00

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