Structure of PDB 2bi3 Chain A

Receptor sequence
>2bi3A (length=360) Species: 1445 (Alkalihalobacillus alcalophilus) [Search protein sequence]
VKQVFNFNAGPSALPKPALERAQKELLNFNDTQMSVMELSHRSQSYEEVH
EQAQNLLRELLQIPNDYQILFLQGGASLQFTMLPMNLLTKGTIGNYVLTG
SWSEKALKEAKLLGETHIAASTKANSYQSIPDFSEFQLNENDAYLHITSN
NTIYGTQYQNFPEINHAPLIADMSSDILSRPLKVNQFGMIYAGAQKNLGP
SGVTVVIVKKDLLNTKVEQVPTMLQYATHIKSDSLYNTPPTFSIYMLRNV
LDWIKDLGGAEAIAKQNEEKAKIIYDTIDESNGFYVGHAEKGSRSLMNVT
FNLRNEELNQQFLAKAKEQGFVGLNGHRSVGGCRASIYNAVPIDACIALR
ELMIQFKENA
3D structure
PDB2bi3 Strain Relief at the Active Site of Phosphoserine Aminotransferase Induced by Radiation Damage.
ChainA
Resolution1.69 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) W102 D172 K196
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 A76 S77 W102 T152 D172 S174 Q195 K196 A76 S77 W102 T152 D172 S174 Q195 K196
BS02 PLP A N237 T238 N237 T238
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:2bi3, PDBe:2bi3, PDBj:2bi3
PDBsum2bi3
PubMed15883191
UniProtQ9RME2|SERC_ALKAL Phosphoserine aminotransferase (Gene Name=serC)

[Back to BioLiP]