Structure of PDB 2c0r Chain B

Receptor sequence

>2c0rB (length=361) Species: 1397 (Niallia circulans)

SERAYNFNAGPAALPLEVLERAQAEFVDYQHTGMSIMEMSHRGAVYEAVH
NEAQARLLALLGNPTGYKVLFIQGGASTQFAMIPMNFLKEGQTANYVMTG
SWASKALKEAKLIGDTHVAASSEASNYMTLPKLQEIQLQDNAAYLHLTSN
ETIEGAQFKAFPDTGSVPLIGDMSSDILSRPFDLNQFGLVYAGAQKNLGP
SGVTVVIVREDLVAESPKHLPTMLRYDTYVKNNSLYNTPPSFGIYMVNEV
LKWIEERGGLEGVQQANRKKASLIYDAIDQSGGFYRGCVDVDSRSDMNIT
FRLASEELEKEFVKASEQEGFVGLKGHRSVGGLRASIYNAVPYESCEALV
QFMEHFKRSRG

3D structure

• PDB: 2c0r Effect of Ph on the Structure and Stability of Bacillus Circulans Ssp. Alkalophilus Phosphoserine Aminotransferase: Thermodynamic and Crystallographic Studies.
• Chain: B
• Resolution: 1.2 Å

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	B	N238 T239	N237 T238
BS02	PLP	B	G76 A77 S78 W103 T153 D173 S175 Q196 K197	G75 A76 S77 W102 T152 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

External links

• PDB: RCSB:2c0r, PDBe:2c0r, PDBj:2c0r
• PDBsum: 2c0r
• PubMed: 16532449
• UniProt: Q59196|SERC_NIACI Phosphoserine aminotransferase (Gene Name=serC)