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2WE4

Carbamate kinase from Enterococcus faecalis bound to a sulfate ion and two water molecules, which mimic the substrate carbamyl phosphate

Summary for 2WE4
Entry DOI10.2210/pdb2we4/pdb
Related2WE5
DescriptorCARBAMATE KINASE 1, SULFATE ION (3 entities in total)
Functional Keywordsarginine catabolism, arginine metabolism, atp synthesys, kinase, open alpha/beta sheet, phosphotransferase, transferase
Biological sourceENTEROCOCCUS FAECALIS
Total number of polymer chains4
Total formula weight133275.26
Authors
Ramon-Maiques, S.,Marina, A.,Gil-Ortiz, F.,Rubio, V. (deposition date: 2009-03-27, release date: 2010-03-16, Last modification date: 2023-12-13)
Primary citationRamon-Maiques, S.,Marina, A.,Guinot, A.,Gil-Ortiz, F.,Uriarte, M.,Fita, I.,Rubio, V.
Substrate Binding and Catalysis in Carbamate Kinase Ascertained by Crystallographic and Site-Directed Mutagenesis Studies. Movements and Significance of a Unique Globular Subdomain of This Key Enzyme for Fermentative ATP Production in Bacteria.
J.Mol.Biol., 397:1261-, 2010
Cited by
PubMed: 20188742
DOI: 10.1016/J.JMB.2010.02.038
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.02 Å)
Structure validation

217705

數據於2024-03-27公開中

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