Brand  (β version)

color scheme of protein:


interaction residue:

chain: Hide other chain(s)

Code Name Link
0JO 2-{[(E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}prop-2-enoic acid
GOL Glycerol
KOU (E)-N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)-L-serine
PYR Pyruvic acid
SER Serine
SO4 Sulfate ion
Code : 4IY7   PDBj   RCSB PDB   PDBe
Header : LYASE
Title : crystal structure of cystathionine gamma lyase (XometC) from Xanthomonas oryzae pv. oryzae in complex with E-site serine, A-site external aldimine structure with serine and A-site external aldimine structure with aminoacrylate intermediates
Release Data : 2014-01-29
Compound :
mol_id molecule chains
1 Cystathionine gamma-lyase-like protein A,B,C,D
Source :
mol_id organism_scientific expression_system
1 Xanthomonas oryzae pv. oryzae  (taxid:291331) Escherichia coli  (taxid:562)
strain: KACC 10331/KXO85
gene: metB, XOCGL, XOO0778
Authors : Ngo, H.P.T., Kim, J.K., Kang, L.W.
Keywords : XOCGL, SERINE EXTERNAL SCHIFF BASE, AMINOACRYLATE EXTERNAL SCHIFF BASE, PLP DEPENDENT ENZYME, LYASE, Cys-Met metabolism PLP dependent enzyme, cystathionine gamma lyase, PLP binding
Exp. method : X-RAY DIFFRACTION ( 1.70 Å )
Citation :

PLP undergoes conformational changes during the course of an enzymatic reaction.

Ngo, H.P.,Cerqueira, N.M.,Kim, J.K.  et al.
(2014)  Acta Crystallogr.,Sect.D  70 : 596 - 606

PubMed: 24531493
DOI: 10.1107/S1399004713031283

Chain : A, B, C, D
UniProt : Q5H4T8 (No found in current UniProtKB/SwissProt)
Reaction : -