Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

5VRH

Apolipoprotein N-acyltransferase C387S active site mutant

Summary for 5VRH
Entry DOI10.2210/pdb5vrh/pdb
Related5VRG
DescriptorApolipoprotein N-acyltransferase, (2S)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate, MAGNESIUM ION, ... (7 entities in total)
Functional Keywordslnt c387s, acyl transferase, membrane protein, transferase
Biological sourceEscherichia coli (strain K12)
Cellular locationCell inner membrane ; Multi- pass membrane protein : P23930
Total number of polymer chains1
Total formula weight60185.21
Authors
Murray, J.M.,Noland, C.L. (deposition date: 2017-05-10, release date: 2017-07-12, Last modification date: 2023-10-04)
Primary citationNoland, C.L.,Kattke, M.D.,Diao, J.,Gloor, S.L.,Pantua, H.,Reichelt, M.,Katakam, A.K.,Yan, D.,Kang, J.,Zilberleyb, I.,Xu, M.,Kapadia, S.B.,Murray, J.M.
Structural insights into lipoprotein N-acylation by Escherichia coli apolipoprotein N-acyltransferase.
Proc. Natl. Acad. Sci. U.S.A., 114:E6044-E6053, 2017
Cited by
PubMed: 28698362
DOI: 10.1073/pnas.1707813114
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.137 Å)
Structure validation

217705

건을2024-03-27부터공개중

PDB statisticsPDBj update infoContact PDBjnumon