EMD-52420

Single-particle
3.54 Å
EMD-52420 Deposition: 23/12/2024
Map released: 14/01/2026
Last modified: 08/04/2026
Overview 3D View Sample Experiment Validation Additional data Links
Overview 3D View Sample Experiment Validation Additional data Links

EMD-52420

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) Map-9huy summary report (pdf.gz) Map-9huy FULL report (pdf.gz)

EMDB Annotations

EMICSS entry mapping (xml)

EMDB Files

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

CryoEM map of the large glutamate dehydrogenase composed of 180 kDa subunits from Mycobacterium smegmatis obtained in the presence of NAD+ and L-glutamate. Closed1 tetramer.

EMD-52420

Single-particle
3.54 Å
EMD-52420 Deposition: 23/12/2024
Map released: 14/01/2026
Last modified: 08/04/2026
Overview 3D View Sample Experiment Validation Additional data Links
Sample Organism: Mycolicibacterium smegmatis
Sample: NAD-specific glutamate dehydrogenase from Mycobacterium smegmatis, MsLGDH180, in the presence of NAD+ and L-glutamate
Fitted models: 9huy

Deposition Authors: Lazaro M , Chamorro N, Lopez-Alonso JP, Charro D, Rasia RM , Jimenez-Oses G, Valle M, Lisa MN
Tertiary and quaternary structure remodeling by occupancy of the substrate binding pocket in a large glutamate dehydrogenase.
Lazaro M , Chamorro N, Lopez-Alonso JP, Charro D, Rasia RM , Jimenez-Oses G, Valle M, Lisa MN
(2026) Protein Sci , 35 , e70544 - e70544
PUBMED: 41877587
DOI: doi:10.1002/pro.70544
ISSN: 1469-896X
ASTM: PRCIEI