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Crystal structure of the L52M mutant of ACRIIA1

Analyse Crystal structure of the L52M mutant of ACRIIA1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5Y69
Type
protein
Length
292 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Chain a
Pockets
3 · best druggability 0.36

Structure

x-ray diffraction · 2 distinct chains · 72% helix, 1% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AChain aprotein14773% helix, 1% strand—
BChain aprotein14570% helix, 1% strand—

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1780.360.7621empty
2730.350.7717empty
3750.320.7417empty

Interfaces

1 interface between chains.

  • A–B · 1357 Ų buried · 19 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 modified (engineered).

Compared structures

  • 5Y69 · Crystal structure of the L52M mutant of AcrIIA1 · the same entry in another collection · chain A against A, TM-score 1.00

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