Structure of PDB 2big Chain B

Receptor sequence

>2bigB (length=355) Species: 1445 (Alkalihalobacillus alcalophilus)

QVFNFNAGPSALPKPALERAQKELLNFNDTQMSVMELSHRSQSYEEVHEQ
AQNLLRELLQIPNDYQILFLQGGASLQFTMLPMNLLTKGTIGNYVLTGSW
SEKALKEAKLLGETHIAASTKANSYQSIPDFSEFQLNENDAYLHITSNNT
IYGTQYQNFPEINHAPLIADMSSDILSRPLKVNQFGMIYAGAQKNLGPSG
VTVVIVKKDLLVEQVPTMLQYATHIKSDSLYNTPPTFSIYMLRNVLDWIK
DLGGAEAIAKQNEEKAKIIYDTIDESNGFYVGHAEKGSRSLMNVTFNLRN
EELNQQFLAKAKEQGFVGLNGHRSVGGCRASIYNAVPIDACIALRELMIQ
FKENA

3D structure

• PDB: 2big Strain Relief at the Active Site of Phosphoserine Aminotransferase Induced by Radiation Damage.
• Chain: B
• Resolution: 1.3 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): W102 D172 K196
• Catalytic site (residue number reindexed from 1): W100 D170 K194
• 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	N237 T238	N232 T233
BS02	PLP	B	A76 S77 W102 T152 D172 S174 Q195 K196	A74 S75 W100 T150 D170 S172 Q193 K194
BS03	MG	B	Y127 Y154 H288	Y125 Y152 H283

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:2big, PDBe:2big, PDBj:2big
• PDBsum: 2big
• PubMed: 15883191
• UniProt: Q9RME2|SERC_ALKAL Phosphoserine aminotransferase (Gene Name=serC)