Brand  (β version)

color scheme of protein:

hetatm:

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information
centroid:
interaction residue:

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Ligands
Code Name Link
CG 4-amidinoindan-1-one-2'-amidinohydrazone
PUT 1,4-diaminobutane
Modified Residues
Code Name Link
MSE Selenomethionine
PYR Pyruvic acid
Code : 1I7M
Header : LYASE
Title : HUMAN S-ADENOSYLMETHIONINE DECARBOXYLASE WITH COVALENTLY BOUND PYRUVOYL GROUP AND COMPLEXED WITH 4-AMIDINOINDAN-1-ONE-2'-AMIDINOHYDRAZONE
Release Data : 2001-08-22
Compound :
mol_id molecule chains
1 S-ADENOSYLMETHIONINE DECARBOXYLASE BETA CHAIN B,D
ec: 4.1.1.50
mol_id molecule chains
2 S-ADENOSYLMETHIONINE DECARBOXYLASE ALPHA CHAIN A,C
ec: 4.1.1.50
Source :
mol_id organism_scientific organism_common expression_system
1 Homo sapiens  (taxid:9606) Human Escherichia coli  (taxid:562)
mol_id organism_scientific organism_common expression_system
2 Homo sapiens  (taxid:9606) Human Escherichia coli  (taxid:562)
Authors : Tolbert, W.D., Ekstrom, J.L., Mathews, I.I., Secrist III, J.A., Pegg, A.E., Ealick, S.E.
Keywords : Spermidine biosynthesis, Lyase, Decarboxylase, Pyruvate, S-ADENOSYLMETHIONINE, SANDWICH, ALLOSTERIC ENZYME, PYRUVOYL
Exp. method : X-RAY DIFFRACTION ( 2.24 Å )
Citation :

The structural basis for substrate specificity and inhibition of human S-adenosylmethionine decarboxylase.

Tolbert, W.D.,Ekstrom, J.L.,Mathews, I.I.  et al.
(2001)  Biochemistry  40 : 9484 - 9494

PubMed: 11583147
DOI: 10.1021/bi010735w

The Crystal Structure of Human S-adenosylmethionine Decarboxylase at 2.25 A Resolution Reveals a Novel Fold

Ekstrom, J.L.,Mathews, I.I.,Stanley, B.A.  et al.
(1999)  Structure  7 : 583 - 595

DOI: 10.1016/S0969-2126(99)80074-4

Chain : A, C
UniProt : P17707 (DCAM_HUMAN)
Reaction : S-adenosyl-L-methionine = S-adenosyl 3- (methylthio)propylamine + CO(2).