1S4D

Crystal Structure Analysis of the S-adenosyl-L-methionine dependent uroporphyrinogen-III C-methyltransferase SUMT

Summary for 1S4D

• Entry DOI: 10.2210/pdb1s4d/pdb
• Descriptor: Uroporphyrin-III C-methyltransferase, S-ADENOSYL-L-HOMOCYSTEINE, GLYCEROL, ... (4 entities in total)
• Functional Keywords: tetrapyrrole biosynthesis, cobalamin, sam, sah, uroporphyrinogen-iii methyltransferase, transferase
• Biological source: Pseudomonas denitrificans
• Total number of polymer chains: 12
• Total formula weight: 358448.72

Authors

Vevodova, J.,Graham, R.M.,Raux, E.,Schubert, H.L.,Roper, D.I.,Brindley, A.A.,Scott, A.I.,Roessner, C.A.,Stamford, N.P.J.,Stroupe, M.E.,Getzoff, E.D.,Warren, M.J.,Wilson, K.S. (deposition date: 2004-01-16, release date: 2004-11-30, Last modification date: 2023-10-25)

• Primary citation: Vevodova, J.,Graham, R.M.,Raux, E.,Schubert, H.L.,Roper, D.I.,Brindley, A.A.,Scott, A.I.,Roessner, C.A.,Stamford, N.P.J.,Stroupe, M.E.,Getzoff, E.D.,Warren, M.J.,Wilson, K.S.; Structure/Function Studies on a S-Adenosyl-l-methionine-dependent Uroporphyrinogen III C Methyltransferase (SUMT), a Key Regulatory Enzyme of Tetrapyrrole Biosynthesis; J.Mol.Biol., 344:419-433, 2004; PubMed: 15522295; DOI: 10.1016/j.jmb.2004.09.020

Experimental method

X-RAY DIFFRACTION (2.7 Å)