› 1i7m

X-ray diffraction
2.24Å resolution

HUMAN S-ADENOSYLMETHIONINE DECARBOXYLASE WITH COVALENTLY BOUND PYRUVOYL GROUP AND COMPLEXED WITH 4-AMIDINOINDAN-1-ONE-2'-AMIDINOHYDRAZONE

Released:
DOI: 10.2210/pdb1i7m/pdb
PDB entry 1i7m coloured by chain, front view.
PDB entry 1i7m coloured by chain, side view.
PDB entry 1i7m coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The structural basis for substrate specificity and inhibition of human S-adenosylmethionine decarboxylase.
Tolbert WD, Ekstrom JL, Mathews II, Secrist JA, Kapoor P, Pegg AE, Ealick SE
Biochemistry 40 9484-94 (2001)
PMID: 11583147

Function and Biology Details

Reaction catalysed: 
S-adenosyl-L-methionine = S-adenosyl 3-(methylthio)propylamine + CO(2)
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assemblies composition:
hetero tetramer
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148140 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
S-adenosylmethionine decarboxylase beta chain Chains: B, D
Molecule details ›
Chains: B, D
Length: 67 amino acids
Theoretical weight: 7.74 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P17707 (Residues: 1-67; Coverage: 20%)
Gene names: AMD, AMD1
Structure domains: S-adenosylmethionine decarboxylase
S-adenosylmethionine decarboxylase alpha chain Chains: A, C
Molecule details ›
Chains: A, C
Length: 267 amino acids
Theoretical weight: 31.19 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P17707 (Residues: 69-334; Coverage: 80%)
Gene names: AMD, AMD1
Sequence domains: Adenosylmethionine decarboxylase
Structure domains: S-adenosylmethionine decarboxylase

Ligands and Environments

2 bound ligands:
Ligand PUT 2 x PUT
Ligand CG 2 x CG
1 modified residue:
Ligand MSE 24 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE F2
Spacegroup: P21
Unit cell:
a: 73.899Å b: 55.672Å c: 96.086Å
α: 90° β: 110.39° γ: 90°
R-values:
R R work R free
0.242 0.242 0.294
Expression system: Escherichia coli

Quick links

Citations

9 review citations

Targeting polyamine metabolism and function in cancer and other hyperproliferative diseases.
Casero et al. (2007)
8 more

6 mentions without citation

Polyamine homoeostasis as a drug target in pathogenic protozoa: peculiarities and possibilities.
Birkholtz et al. (2011)
5 more