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9YX5

Structure of the long chain acyl-CoA carboxylase complex from Mycobacterium smegmatis with MSMEG_0435-MSMEG_0436 bound

This is a non-PDB format compatible entry.
Summary for 9YX5
Entry DOI10.2210/pdb9yx5/pdb
EMDB information73596
DescriptorBiotin-dependent acyl-coenzyme A carboxylase alpha3 subunit, BICARBONATE ION, ADENOSINE-5'-TRIPHOSPHATE, ... (12 entities in total)
Functional Keywordscarboxylase, transferase, lipid synthesis, mycolic acid synthesis, ligase
Biological sourceMycolicibacterium smegmatis MC2 155
More
Total number of polymer chains26
Total formula weight1367841.29
Authors
Liang, Y.,Rubinstein, J.L. (deposition date: 2025-10-26, release date: 2025-11-26)
Primary citationLiang, Y.,Rubinstein, J.L.
Structural basis for substrate specificity and MSMEG_0435-0436 binding by the mycobacterial long-chain acyl-CoA carboxylase complex
To Be Published,
Experimental method
ELECTRON MICROSCOPY (2.9 Å)
Structure validation

247536

PDB entries from 2026-01-14

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