Structure of PDB 2big Chain A

Receptor sequence
>2bigA (length=358) Species: 1445 (Alkalihalobacillus alcalophilus) [Search protein sequence]
QVFNFNAGPSALPKPALERAQKELLNFNDTQMSVMELSHRSQSYEEVHEQ
AQNLLRELLQIPNDYQILFLQGGASLQFTMLPMNLLTKGTIGNYVLTGSW
SEKALKEAKLLGETHIAASTKANSYQSIPDFSEFQLNENDAYLHITSNNT
IYGTQYQNFPEINHAPLIADMSSDILSRPLKVNQFGMIYAGAQKNLGPSG
VTVVIVKKDLLNTKVEQVPTMLQYATHIKSDSLYNTPPTFSIYMLRNVLD
WIKDLGGAEAIAKQNEEKAKIIYDTIDESNGFYVGHAEKGSRSLMNVTFN
LRNEELNQQFLAKAKEQGFVGLNGHRSVGGCRASIYNAVPIDACIALREL
MIQFKENA
3D structure
PDB2big Strain Relief at the Active Site of Phosphoserine Aminotransferase Induced by Radiation Damage.
ChainA
Resolution1.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 A A76 S77 W102 T152 D172 S174 Q195 K196 A74 S75 W100 T150 D170 S172 Q193 K194
BS02 PLP A N237 T238 N235 T236
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

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Cellular Component
External links
PDB RCSB:2big, PDBe:2big, PDBj:2big
PDBsum2big
PubMed15883191
UniProtQ9RME2|SERC_ALKAL Phosphoserine aminotransferase (Gene Name=serC)

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