Structure of PDB 1bjo Chain B

Receptor sequence

>1bjoB (length=360) Species: 562 (Escherichia coli)

QIFNFSSGPAMLPAEVLKQAQQELRDWNGLGTSVMEVSHRGKEFIQVAEE
AEKDFRDLLNVPSNYKVLFCHGGGRGQFAAVPLNILGDKTTADYVDAGYW
AASAIKEAKKYCTPNVFDAKVTVDGLRAVKPMREWQLSDNAAYMHYCPNE
TIDGIAIDETPDFGADVVVAADFSSTILSRPIDVSRYGVIYAGAQKNIGP
AGLTIVIVREDLLGKANIACPSILDYSILNDNGSMFNTPPTFAWYLSGLV
FKWLKANGGVAEMDKINQQKAELLYGVIDNSDFYRNDVAKRNRSRMNVPF
QLADSALDKLFLEESFAAGLHALKGHRVVGGMRASIYNAMPLEGVKALTD
FMVEFERRHG

3D structure

• PDB: 1bjo 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.
• Chain: B
• Resolution: 2.8 Å

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.

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	B	N239 T240	N237 T238

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

External links

• PDB: RCSB:1bjo, PDBe:1bjo, PDBj:1bjo
• PDBsum: 1bjo
• PubMed: 10024454
• UniProt: P23721|SERC_ECOLI Phosphoserine aminotransferase (Gene Name=serC)