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6I3D

Crystal structure of Human soluble catechol O-methyltransferase in complex with 3,5-dinitrocatechol and Sinefungin

Summary for 6I3D
Entry DOI10.2210/pdb6i3d/pdb
DescriptorCatechol O-methyltransferase, 3,5-DINITROCATECHOL, MAGNESIUM ION, ... (5 entities in total)
Functional Keywordsenzyme, s-adenosyl-l-methionine, catechol o-methyltransferase, transferase
Biological sourceHomo sapiens (Human)
Total number of polymer chains2
Total formula weight53152.83
Authors
Levy, C.W. (deposition date: 2018-11-05, release date: 2019-09-18, Last modification date: 2024-05-01)
Primary citationCzarnota, S.,Johannissen, L.O.,Baxter, N.J.,Rummel, F.,Wilson, A.L.,Cliff, M.J.,Levy, C.W.,Scrutton, N.S.,Waltho, J.P.,Hay, S.
Equatorial Active Site Compaction and Electrostatic Reorganization in Catechol-O-methyltransferase.
Acs Catalysis, 9:4394-4401, 2019
Cited by
PubMed: 31080692
DOI: 10.1021/acscatal.9b00174
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.45 Å)
Structure validation

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