EMD-73586

Single-particle
3.3 Å
EMD-73586
3D View Gallery
Deposition: 26/10/2025
Map released: 26/11/2025
Last modified: 01/04/2026
Overview 3D View Sample Experiment Validation Additional data Links
Overview 3D View Sample Experiment Validation Additional data Links

EMD-73586

Archive Files (Depositor)

Primary 3D volume (map.gz) Half-map 1 Half-map 2 (map.gz) Experimental metadata (xml) Experimental metadata (cif.gz)

Validation (wwPDB)

Map-only validation report (pdf.gz)

EMDB Annotations

EMICSS entry mapping (xml)

EMDB Files

VA raw map (map) VA resolution mask (mrc)

Locally refined map of the left BCCP in the up conformation of the long chain acyl-CoA carboxylase complex from Mycobacterium smegmatis with ATP, bicarbonate, and propionyl-CoA

EMD-73586

Single-particle
3.3 Å
EMD-73586
3D View Gallery
Deposition: 26/10/2025
Map released: 26/11/2025
Last modified: 01/04/2026
Overview 3D View Sample Experiment Validation Additional data Links
Sample Organism: Mycolicibacterium smegmatis MC2 155
Sample: Locally refined map of the left BCCP in the up conformation of the long chain acyl-CoA carboxylase complex from Mycobacterium smegmatis with ATP, bicarbonate, and propionyl-CoA

Deposition Authors: Liang Y , Rubinstein JL
Structural basis for substrate specificity and MSMEG_0435-0436 binding by the mycobacterial long-chain acyl-CoA carboxylase complex.
Liang Y , Bueler SA, Rubinstein JL
(2026) PNAS , 123 , e2530575123 - e2530575123
PUBMED: 41843674
DOI: doi:10.1073/pnas.2530575123
ISSN: 1091-6490
ASTM: PNASA6