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Crystal structure of a novel engineered retroaldolase: ra-22

Analyse Crystal structure of a novel engineered retroaldolase: ra-22 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3HOJ
Type
protein
Length
247 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Retroaldolase-22
EC
4.1.1.48
Pockets
2 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 17% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ARetroaldolase-22 (EC 4.1.1.48)protein24738% helix, 17% strand—

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12700.760.8939empty
2520.230.7213empty

Compared structures

  • 3HOJ · Crystal Structure of a Novel Engineered Retroaldolase: RA-22 · the same entry in another collection · chain A against A, TM-score 1.00

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