Structure of PDB 1bt4 Chain A

Receptor sequence
>1bt4A (length=361) Species: 1397 (Niallia circulans) [Search protein sequence]
SERAYNFNAGPAALPLEVLERAQAEFVDYQHTGMSIMEMSHRGAVYEAVH
NEAQARLLALLGNPTGYKVLFIQGGASTQFAMIPMNFLKEGQTANYVMTG
SWASKALKEAKLIGDTHVAASSEASNYMTLPKLQEIQLQDNAAYLHLTSN
ETIEGAQFKAFPDTGSVPLIGDMSSDILSRPFDLNQFGLVYAGAQKNLGP
SGVTVVIVREDLVAESPKHLPTMLRYDTYVKNNSLYNTPPSFGIYMVNEV
LKWIEERGGLEGVQQANRKKASLIYDAIDQSGGFYRGCVDVDSRSDMNIT
FRLASEELEKEFVKASEQEGFVGLKGHRSVGGLRASIYNAVPYESCEALV
QFMEHFKRSRG
3D structure
PDB1bt4 Phosphoserine Aminotransferase from Bacillus Circulans Subsp. Alkalophilus: Purification, Gene Cloning and Sequencing
ChainA
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) W103 D173 K197
Catalytic site (residue number reindexed from 1) W102 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 A A77 S78 W103 D173 S175 Q196 K197 A76 S77 W102 D172 S174 Q195 K196
Gene Ontology
Molecular Function
GO:0004648 O-phospho-L-serine:2-oxoglutarate aminotransferase activity
GO:0008483 transaminase activity
GO:0030170 pyridoxal phosphate binding
Biological Process
GO:0006563 L-serine metabolic process
GO:0006564 L-serine biosynthetic process
Cellular Component
GO:0005737 cytoplasm

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1bt4, PDBe:1bt4, PDBj:1bt4
PDBsum1bt4
PubMed
UniProtQ59196|SERC_NIACI Phosphoserine aminotransferase (Gene Name=serC)

[Back to BioLiP]