Structure of PDB 1bjo Chain B Binding Site BS01

Receptor Information
>1bjo Chain B (length=360) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
QIFNFSSGPAMLPAEVLKQAQQELRDWNGLGTSVMEVSHRGKEFIQVAEE
AEKDFRDLLNVPSNYKVLFCHGGGRGQFAAVPLNILGDKTTADYVDAGYW
AASAIKEAKKYCTPNVFDAKVTVDGLRAVKPMREWQLSDNAAYMHYCPNE
TIDGIAIDETPDFGADVVVAADFSSTILSRPIDVSRYGVIYAGAQKNIGP
AGLTIVIVREDLLGKANIACPSILDYSILNDNGSMFNTPPTFAWYLSGLV
FKWLKANGGVAEMDKINQQKAELLYGVIDNSDFYRNDVAKRNRSRMNVPF
QLADSALDKLFLEESFAAGLHALKGHRVVGGMRASIYNAMPLEGVKALTD
FMVEFERRHG
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 chain1bjo Chain A Residue 363 [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]
PDB1bjo Crystal structure of phosphoserine aminotransferase from Escherichia coli at 2.3 A resolution: comparison of the unligated enzyme and a complex with alpha-methyl-l-glutamate.
Resolution2.8 Å
Binding residue
(original residue number in PDB)		N239 T240
Binding residue
(residue number reindexed from 1)		N237 T238
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) W102 D174 K198
Catalytic site (residue number reindexed from 1) W100 D172 K196
Enzyme Commision number 2.6.1.52: phosphoserine transaminase.
Gene Ontology
Molecular Function
GO:0004648 O-phospho-L-serine:2-oxoglutarate aminotransferase activity
GO:0005515 protein binding
GO:0008483 transaminase activity
GO:0030170 pyridoxal phosphate binding
GO:0042803 protein homodimerization activity
Biological Process
GO:0006563 L-serine metabolic process
GO:0006564 L-serine biosynthetic process
GO:0008615 pyridoxine biosynthetic process
GO:0033359 lysine biosynthetic process via diaminopimelate and N-succinyl-2-amino-6-ketopimelate
GO:0042823 pyridoxal phosphate biosynthetic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1bjo, PDBe:1bjo, PDBj:1bjo
PDBsum1bjo
PubMed10024454
UniProtP23721|SERC_ECOLI Phosphoserine aminotransferase (Gene Name=serC)

[Back to BioLiP]