Structure of PDB 1pwh Chain B Binding Site BS01

Receptor Information
>1pwh Chain B (length=327) Species: 10116 (Rattus norvegicus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MAAQESLHVKTPLRDSMALSKVAGTSVFLKMDSSQPSGSFKIRGIGHLCK
MKAKQGCKHFVCSSAGNAGMATAYAARRLGLPATIVVPSTTPALTIERLK
NEGATVEVVGEMLDEAIQLAKALEKNNPGWVYISPFDDPLIWEGHTSLVK
ELKETLSAKPGAIVLSVGGGGLLCGVVQGLREVGWEDVPIIAMETFGAHS
FHAAVKEGKLVTLPKITSVAKALGVNTVGAQTLKLFYEHPIFSEVISDQE
AVTAIEKFVDDEKILVEPACGAALAAVYSGVVCRLQAEARLQTPLASLVV
IVCGGSNISLAQLQALKAQLGLNELLK
Ligand information
Ligand IDPLV
InChIInChI=1S/C12H19N2O8P/c1-7-11(15)9(4-14-10(6-21-2)12(16)17)8(3-13-7)5-22-23(18,19)20/h3,10,14-15H,4-6H2,1-2H3,(H,16,17)(H2,18,19,20)/t10-/m0/s1
InChIKeyDEHSEGNQBACQEW-JTQLQIEISA-N
SMILES
SoftwareSMILES
CACTVS 3.341COC[C@H](NCc1c(O)c(C)ncc1CO[P](O)(O)=O)C(O)=O
ACDLabs 10.04O=C(O)C(NCc1c(cnc(c1O)C)COP(=O)(O)O)COC
OpenEye OEToolkits 1.5.0Cc1c(c(c(cn1)COP(=O)(O)O)CNC(COC)C(=O)O)O
CACTVS 3.341COC[CH](NCc1c(O)c(C)ncc1CO[P](O)(O)=O)C(O)=O
OpenEye OEToolkits 1.5.0Cc1c(c(c(cn1)COP(=O)(O)O)CN[C@@H](COC)C(=O)O)O
FormulaC12 H19 N2 O8 P
NameN-({3-HYDROXY-2-METHYL-5-[(PHOSPHONOOXY)METHYL]PYRIDIN-4-YL}METHYL)-O-METHYL-L-SERINE;
PYRIDOXYL-(O-METHYL-SERINE)-5-MONOPHOSPHATE
ChEMBL
DrugBank
ZINCZINC000002047394
PDB chain1pwh Chain B Residue 329 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1pwh Crystal structure of serine dehydratase from rat liver.
Resolution2.6 Å
Binding residue
(original residue number in PDB)		F40 K41 S64 A65 N67 A68 F136 G168 G169 G170 G171 A222 G224 C303 G304
Binding residue
(residue number reindexed from 1)		F40 K41 S64 A65 N67 A68 F136 G168 G169 G170 G171 A222 G224 C303 G304
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) K41 A65 E194 A198 S200 A222 A269 C303
Catalytic site (residue number reindexed from 1) K41 A65 E194 A198 S200 A222 A269 C303
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: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:0031667 response to nutrient levels
GO:0033590 response to cobalamin
GO:0042866 pyruvate biosynthetic process
GO:0043200 response to amino acid
GO:0065003 protein-containing complex assembly
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1pwh, PDBe:1pwh, PDBj:1pwh
PDBsum1pwh
PubMed14596599
UniProtP09367|SDHL_RAT L-serine dehydratase/L-threonine deaminase (Gene Name=Sds)

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