Structure of PDB 1p5j Chain A Binding Site BS01

Receptor Information
>1p5j Chain A (length=319) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
GEPLHVKTPIRDSMALSKMAGTSVYLKMDSAQPSGSFKIRGIGHFCKRWA
KQGCAHFVCSSAGNAGMAAAYAARQLGVPATIVVPGTTPALTIERLKNEG
ATCKVVGELLDEAFELAKALAKNNPGWVYIPPFDDPLIWEGHASIVKELK
ETLWEKPGAIALSVGGGGLLCGVVQGLQECGWGDVPVIAMETFGAHSFHA
ATTAGKLVSLPKITSVAKALGVKTVGSQALKLFQEHPIFSEVISDQEAVA
AIEKFVDDEKILVEPACGAALAAVYSHVIQKLQLEGNLRTPLPSLVVIVC
GGSNISLAQLRALKEQLGM
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 chain1p5j Chain A Residue 941 [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]
PDB1p5j Crystallization and preliminary crystallographic analysis of human serine dehydratase.
Resolution2.5 Å
Binding residue
(original residue number in PDB)		F40 K41 N67 V167 G168 G169 G170 G171 A222 C303 G304 G305
Binding residue
(residue number reindexed from 1)		F37 K38 N64 V164 G165 G166 G167 G168 A219 C300 G301 G302
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) K41 A65 E194 A198 S200 A222 C303
Catalytic site (residue number reindexed from 1) K38 A62 E191 A195 S197 A219 C300
Enzyme Commision number 4.3.1.17: L-serine ammonia-lyase.
4.3.1.19: threonine ammonia-lyase.
Gene Ontology
Molecular Function
GO:0003941 L-serine ammonia-lyase activity
GO:0004794 threonine deaminase activity
GO:0005515 protein binding
GO:0016829 lyase activity
GO:0030170 pyridoxal phosphate binding
GO:0042803 protein homodimerization activity
Biological Process
GO:0006094 gluconeogenesis
GO:0006520 amino acid metabolic process
GO:0006565 L-serine catabolic process
GO:0006567 threonine catabolic process
GO:0006629 lipid metabolic process
GO:0009097 isoleucine biosynthetic process
GO:0042866 pyruvate biosynthetic process
Cellular Component
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005829 cytosol

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1p5j, PDBe:1p5j, PDBj:1p5j
PDBsum1p5j
PubMed14646100
UniProtP20132|SDHL_HUMAN L-serine dehydratase/L-threonine deaminase (Gene Name=SDS)

[Back to BioLiP]