Brand  (β version)

PDB ID: 1MSV

Hetero Atom Contents

  The number of atoms exceeds 100,000.
  So, it can not be displayed here.

Select unit:

Select hetatm:   

close
information
centroid:
interaction residue:

Select chain:   Sequence  

Data format:   

Color scheme of protein:

Ligands
Code Name Style Show Link
PUT 1,4-diaminobutane PoSSuM
TRS 2-amino-2-hydroxymethyl-propane-1,3-diol PoSSuM
Non-standard Residues
Code Name Show
Glycosylation
Code Name Emphasize
Modification
Code Name Show

Structure summary

Code : 1MSV   PDBj   RCSB PDB   PDBe
Header : LYASE
Title : The S68A S-adenosylmethionine decarboxylase proenzyme processing mutant.
Release Data : 2003-03-11
Compound :
mol_id molecule chains synonym
1 S-adenosylmethionine decarboxylase proenzyme A,B AdoMetDC, SamDC
ec: 4.1.1.50
mutation: S68A
Source :
mol_id organism_scientific organism_common expression_system
1 Homo sapiens  (taxid:9606) Human Escherichia coli  (taxid:562)
expression_system_strain: XL-1 Blue/JM109
expression_system_vector_type: plasmid
expression_system_plasmid: pQE30 (Qiagen)
Authors : Tolbert, W.D., Zhang, Y., Bennett, E.M., Cottet, S.E., Ekstrom, J.L., Pegg, A.E., Ealick, S.E.
Keywords : spermidine biosynthesis, lyase, decarboxylase, pyruvate, s-adenosylmethionine, sandwich, allosteric enzyme, pyruvoyl
Exp. method : X-RAY DIFFRACTION ( 1.75 Å )
Citation :

Mechanism of Human S-Adenosylmethionine Decarboxylase Proenzyme Processing as Revealed by the Structure of the S68A Mutant.

Tolbert, W.D.,Zhang, Y.,Cottet, S.E.  et al.
(2003)  Biochemistry  42 : 2386 - 2395

PubMed: 12600205
DOI: 10.1021/bi0268854

Structure of a Human S-Adenosylmethionine Decarboxylase Self-Processing Ester Intermediate and Mechanism of Putrescine Stimulation of Processing As Revealed by the H243A Mutant

Ekstrom, J.L.,Tolbert, W.D.,Xiong, H.  et al.
(2001)  Biochemistry  40 : 9495 - 9504

DOI: 10.1021/bi010736o

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

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

Reaction

Chain : A, B
UniProt : P17707 (DCAM_HUMAN)
Reaction: EC: Evidence:
Physiological Direction:
H(+) + S-adenosyl-L-methionine = CO2 + S-adenosyl 3- (methylsulfanyl)propylamine 4.1.1.50 PubMed:10029540, PubMed:10574985, PubMed:11583147, PubMed:1917972, PubMed:2460457, PubMed:2687270
-