Structure of PDB 1w23 Chain B

Receptor sequence

>1w23B (length=357) Species: 1445 (Alkalihalobacillus alcalophilus)

VKQVFNFNAGPSALPKPALERAQKELLNFNDTQMSVMELSHRSQSYEEVH
EQAQNLLRELLQIPNDYQILFLQGGASLQFTMLPMNLLTKGTIGNYVLTG
SWSEKALKEAKLLGETHIAASTKANSYQSIPDFSEFQLNENDAYLHITSN
NTIYGTQYQNFPEINHAPLIADMSSDILSRPLKVNQFGMIYAGAQKNLGP
SGVTVVIVKKDLLVEQVPTMLQYATHIKSDSLYNTPPTFSIYMLRNVLDW
IKDLGGAEAIAKQNEEKAKIIYDTIDESNGFYVGHAEKGSRSLMNVTFNL
RNEELNQQFLAKAKEQGFVGLNGHRSVGGCRASIYNAVPIDACIALRELM
IQFKENA

3D structure

• PDB: 1w23 Enzyme Adaptation to Alkaline Ph: Atomic Resolution (1.08 A) Structure of Phosphoserine Aminotransferase from Bacillus Alcalophilus
• Chain: B
• Resolution: 1.08 Å

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	B	N237 T238	N234 T235
BS02	MG	B	Y127 Y154 H288 A289	Y127 Y154 H285 A286
BS03	PLP	B	A76 S77 W102 T152 D172 S174 Q195 K196	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:1w23, PDBe:1w23, PDBj:1w23
• PDBsum: 1w23
• PubMed: 15608117
• UniProt: Q9RME2|SERC_ALKAL Phosphoserine aminotransferase (Gene Name=serC)