Structure of PDB 8biz Chain E

Receptor sequence
>8bizE (length=389) Species: 5811 (Toxoplasma gondii) [Search protein sequence]
KAGDWLPGFTPREETVYVHGGVEPDPLTGAILPPIYQNTTFVQESVENYL
SKGFSYSRTSNPTVLSLEKKIAEIEGGFGACCFATGMAATVTIFSAFLAP
GDHCLVTNCSYGGTNRCARLHFSKYNIDFEFIDFRDPTNVEKAIRPQTKV
VFSESPCNPTLYLADIEAISQICKEKKVLHVCDSTFATPYMMRPLDLGAD
IVVQSTTKYYDGHNCTLGGAVISSTKEIHDKVFFLRNVMGNIMSAQTAFY
TLLTLKTLPIRVEKQSANAQKIAEFLSKHHKVEHVIYPGIPSFPQKELAL
KQHKNVHGGMLAFEVKGGTEAGIRMMNHVPRPWSLCESLGACESIITCPA
VFREDRLKVGITDGFIRVSVGIEDVNDLIDGLDYALSKA
3D structure
PDB8biz Structural basis of the inhibition of cystathionine gamma-lyase from Toxoplasma gondii by propargylglycine and cysteine.
ChainE
Resolution1.891 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 4.4.1.1: cystathionine gamma-lyase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 PLP E G108 M109 Y133 D205 S227 T229 K230 G86 M87 Y111 D183 S205 T207 K208
BS02 CYS E Y133 K230 E359 S360 R395 Y111 K208 E337 S338 R367
BS03 PLP E Y78 R80 Y56 R58
Gene Ontology
Molecular Function
GO:0004123 cystathionine gamma-lyase activity
GO:0016829 lyase activity
GO:0016846 carbon-sulfur lyase activity
GO:0030170 pyridoxal phosphate binding
GO:0044540 L-cystine L-cysteine-lyase (deaminating)
GO:0080146 L-cysteine desulfhydrase activity
Biological Process
GO:0019346 transsulfuration
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Cellular Component
External links
PDB RCSB:8biz, PDBe:8biz, PDBj:8biz
PDBsum8biz
PubMed36883335
UniProtB6K8Y1

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