Structure of PDB 1n8p Chain C Binding Site BS01

Receptor Information
>1n8p Chain C (length=393) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
TLQESDKFATKAIHAGEHVDVHGSVIEPISLSTTFKQSSPANPIGTYEYS
RSQNPNRENLERAVAALENAQYGLAFSSGSATTATILQSLPQGSHAVSIG
DVYGGTHRYFTKVANAHGVETSFTNDLLNDLPQLIKENTKLVWIETPTNP
TLKVTDIQKVADLIKKHAAGQDVILVVDNTFLSPYISNPLNFGADIVVHS
ATKYINGHSDVVLGVLATNNKPLYERLQFLQNAIGAIPSPFDAWLTHRGL
KTLHLRVRQAALSANKIAEFLAADKENVVAVNYPGLKTHPNYDVVLKQHR
DALGGGMISFRIKGGAEAASKFASSTRLFTLAESLGGIESLLEVPAVMTH
GGIPKEAREASGVFDDLVRISVGIEDTDDLLEDIKQALKQATN
Ligand information
Ligand IDPLP
InChIInChI=1S/C8H10NO6P/c1-5-8(11)7(3-10)6(2-9-5)4-15-16(12,13)14/h2-3,11H,4H2,1H3,(H2,12,13,14)
InChIKeyNGVDGCNFYWLIFO-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341Cc1ncc(CO[P](O)(O)=O)c(C=O)c1O
OpenEye OEToolkits 1.5.0Cc1c(c(c(cn1)COP(=O)(O)O)C=O)O
ACDLabs 10.04O=P(O)(O)OCc1cnc(c(O)c1C=O)C
FormulaC8 H10 N O6 P
NamePYRIDOXAL-5'-PHOSPHATE;
VITAMIN B6 Phosphate
ChEMBLCHEMBL82202
DrugBankDB00114
ZINCZINC000001532514
PDB chain1n8p Chain C Residue 400 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB1n8p Determinants of Enzymatic Specificity in the Cys-Met-Metabolism PLP-Dependent Enzymes Family: Crystal Structure of Cystathionine gamma-lyase from Yeast and Intrafamiliar Structural Comparison
Resolution2.6 Å
Binding residue
(original residue number in PDB)		S78 G79 S80 Y103 D178 F181 S200 K203
Binding residue
(residue number reindexed from 1)		S78 G79 S80 Y103 D178 F181 S200 K203
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) R51 Y103 D178 K203
Catalytic site (residue number reindexed from 1) R51 Y103 D178 K203
Enzyme Commision number 4.4.1.1: cystathionine gamma-lyase.
Gene Ontology
Molecular Function
GO:0004123 cystathionine gamma-lyase activity
GO:0016829 lyase activity
GO:0030170 pyridoxal phosphate binding
GO:0044540 L-cystine L-cysteine-lyase (deaminating)
GO:0047804 cysteine-S-conjugate beta-lyase activity
GO:0080146 L-cysteine desulfhydrase activity
Biological Process
GO:0019343 cysteine biosynthetic process via cystathionine
GO:0019344 cysteine biosynthetic process
GO:0019346 transsulfuration
GO:1904828 positive regulation of hydrogen sulfide biosynthetic process
Cellular Component
GO:0005634 nucleus
GO:0005737 cytoplasm

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1n8p, PDBe:1n8p, PDBj:1n8p
PDBsum1n8p
PubMed12715888
UniProtP31373|CYS3_YEAST Cystathionine gamma-lyase (Gene Name=CYS3)

[Back to BioLiP]