1I7B

HUMAN S-ADENOSYLMETHIONINE DECARBOXYLASE WITH COVALENTLY BOUND PYRUVOYL GROUP AND COVALENTLY BOUND S-ADENOSYLMETHIONINE METHYL ESTER

Summary for 1I7B

Related1JEN 1I72 1I79 1I7C 1I7M
DescriptorS-ADENOSYLMETHIONINE DECARBOXYLASE BETA CHAIN, S-ADENOSYLMETHIONINE DECARBOXYLASE ALPHA CHAIN, S-ADENOSYLMETHIONINE METHYL ESTER, ... (5 entities in total)
Functional Keywordsspermidine biosynthesis, lyase, decarboxylase, pyruvate, s-adenosylmethionine, sandwich, allosteric enzyme, pyruvoyl
Biological sourceHomo sapiens (human)
Total number of polymer chains2
Total molecular weight38869.17
Authors
Tolbert, W.D.,Ekstrom, J.L.,Mathews, I.I.,Secrist III, J.A.,Pegg, A.E.,Ealick, S.E. (deposition date: 2001-03-08, release date: 2001-08-22, Last modification date: 2018-01-31)
Primary citation
Tolbert, W.D.,Ekstrom, J.L.,Mathews, I.I.,Secrist III, J.A.,Kapoor, P.,Pegg, A.E.,Ealick, S.E.
The structural basis for substrate specificity and inhibition of human S-adenosylmethionine decarboxylase.
Biochemistry, 40:9484-9494, 2001
PubMed: 11583147 (PDB entries with the same primary citation)
DOI: 10.1021/bi010735w
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (1.9 Å)
?

Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers0.23960.7%1.1%8.7%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution