7LNH
S-adenosylmethionine synthetase co-crystallized with UppNHp
Summary for 7LNH
Entry DOI | 10.2210/pdb7lnh/pdb |
Descriptor | S-adenosylmethionine synthase isoform type-2, (2~{S})-2-azanyl-4-[[(2~{S},3~{S},4~{R},5~{R})-5-[2,4-bis(oxidanylidene)pyrimidin-1-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methyl-methyl-$l^{3}-sulfanyl]butanoic acid, 1,2-ETHANEDIOL, ... (4 entities in total) |
Functional Keywords | s-adenosylmethionine synthetase, transferase |
Biological source | Homo sapiens (Human) |
Total number of polymer chains | 2 |
Total formula weight | 88254.11 |
Authors | Tan, L.L.,Jackson, C.J. (deposition date: 2021-02-07, release date: 2022-03-02, Last modification date: 2023-10-18) |
Primary citation | Gade, M.,Tan, L.L.,Damry, A.M.,Sandhu, M.,Brock, J.S.,Delaney, A.,Villar-Briones, A.,Jackson, C.J.,Laurino, P. Substrate Dynamics Contribute to Enzymatic Specificity in Human and Bacterial Methionine Adenosyltransferases. Jacs Au, 1:2349-2360, 2021 Cited by PubMed: 34977903DOI: 10.1021/jacsau.1c00464 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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