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7AC8

Molecular basis for the unique allosteric activation mechanism of the heterodimeric imidazole glycerol phosphate synthase complex.

Summary for 7AC8
Entry DOI10.2210/pdb7ac8/pdb
DescriptorImidazole glycerol phosphate synthase subunit HisF, Imidazole glycerol phosphate synthase subunit HisH, [(2R,3S,4R,5R)-5-[4-aminocarbonyl-5-[(E)-[[(2R,3R,4S,5R)-3,4-bis(oxidanyl)-5-(phosphonooxymethyl)oxolan-2-yl]amino]methylideneamino]imidazol-1-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methyl dihydrogen phosphate, ... (6 entities in total)
Functional Keywordsenzyme regulation, allostery, ensemble model, conformational changes, hisf, hish, imidazole glycerol phosphate synthase, lyase (4.3.2.10), lyase
Biological sourceThermotoga maritima
More
Total number of polymer chains6
Total formula weight154809.91
Authors
Sung, S.,Wilmanns, M. (deposition date: 2020-09-10, release date: 2021-05-19, Last modification date: 2024-01-31)
Primary citationWurm, J.P.,Sung, S.,Kneuttinger, A.C.,Hupfeld, E.,Sterner, R.,Wilmanns, M.,Sprangers, R.
Molecular basis for the allosteric activation mechanism of the heterodimeric imidazole glycerol phosphate synthase complex.
Nat Commun, 12:2748-2748, 2021
Cited by
PubMed: 33980881
DOI: 10.1038/s41467-021-22968-6
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.06 Å)
Structure validation

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