Brand  (β version)

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Ligands
Code Name Link
0JO 2-{[(E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}prop-2-enoic acid
MPD (4s)-2-methyl-2,4-pentanediol
Code : 5B3A   PDBj   RCSB PDB   PDBe
Header : TRANSFERASE
Title : Crystal Structure of O-Phoshoserine Sulfhydrylase from Aeropyrum pernix in Complexed with the alpha-Aminoacrylate Intermediate
Release Data : 2016-03-16
Compound :
mol_id molecule chains synonym
1 Protein CysO A,B Cystathionine beta-synthase,Cysteine synthase,O-acetylserine sulfhydrylase,O-phosphoserine sulfhydrylase,Serine sulfhydrase
ec: 4.2.1.22,2.5.1.47,2.5.1.65
Source :
mol_id organism_scientific expression_system
1 Aeropyrum pernix K1  (taxid:272557) Escherichia coli  (taxid:562)
strain: K1
gene: cysO, APE_1586
expression_system_strain: Rosetta (DE3)
expression_system_vector_type: plasmid
expression_system_plasmid: pET3d
Authors : Nakamura, T., Takeda, E., Kawai, Y., Kataoka, M., Ishikawa, K.
Keywords : Cysteine Biosynthesis, sulfhydrylase, intermediate, External Schiff base of PLP with alpha-amino acrylate, TRANSFERASE
Exp. method : X-RAY DIFFRACTION ( 2.14 Å )
Citation :

Role of F225 in O-phosphoserine sulfhydrylase from Aeropyrum pernix K1

Takeda, E.,Kunimoto, K.,Kawai, Y.  et al.
(2016)  Extremophiles  20 : 733 - 745

PubMed: 27377295
DOI: 10.1007/s00792-016-0862-6

Structural analysis of the substrate recognition mechanism in O-phosphoserine sulfhydrylase from the hyperthermophilic archaeon Aeropyrum pernix K1

Nakamura, T.,Kawai, Y.,Kunimoto, K.  et al.
(2012)  J.Mol.Biol.  422 : 33 - 44

PubMed: 22580223
DOI: 10.1016/j.jmb.2012.05.009

Three-dimensional structure of a new enzyme, O-phosphoserine sulfhydrylase, involved in l-cysteine biosynthesis by a hyperthermophilic archaeon, Aeropyrum pernix K1, at 2.0A resolution

Oda, Y.,Mino, K.,Ishikawa, K.  et al.
(2005)  J.Mol.Biol.  351 : 334 - 344

PubMed: 16005886
DOI: 10.1016/j.jmb.2005.05.064

Chain : A, B
UniProt : Q9YBL2 (CYSO_AERPE)
Reaction : Reaction=hydrogen sulfide + O-acetyl-L-serine = acetate + L-cysteine; Xref=Rhea:RHEA:14829, ChEBI:CHEBI:29919, ChEBI:CHEBI:30089, ChEBI:CHEBI:35235, ChEBI:CHEBI:58340; EC=2.5.1.47; Evidence={ECO:0000269|PubMed:12644499};
Reaction=H(+) + hydrogen sulfide + O-phospho-L-serine = L-cysteine + phosphate; Xref=Rhea:RHEA:10252, ChEBI:CHEBI:15378, ChEBI:CHEBI:29919, ChEBI:CHEBI:35235, ChEBI:CHEBI:43474, ChEBI:CHEBI:57524; EC=2.5.1.65; Evidence={ECO:0000269|PubMed:16005886};
Reaction=L-homocysteine + L-serine = H2O + L,L-cystathionine; Xref=Rhea:RHEA:10112, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384, ChEBI:CHEBI:58161, ChEBI:CHEBI:58199; EC=4.2.1.22; Evidence={ECO:0000269|PubMed:12644499, ECO:0000269|PubMed:16005886};