Structure of PDB 1w3u Chain A

Receptor sequence
>1w3uA (length=360) Species: 1397 (Niallia circulans) [Search protein sequence]
ERAYNFNAGPAALPLEVLERAQAEFVDYQHTGMSIMEMSHRGAVYEAVHN
EAQARLLALLGNPTGYKVLFIQGGASTQFAMIPMNFLKEGQTANYVMTGS
WASKALKEAKLIGDTHVAASSEASNYMTLPKLQEIQLQDNAAYLHLTSNE
TIEGAQFKAFPDTGSVPLIGDMSSDILSRPFDLNQFGLVYAGAQKNLGPS
GVTVVIVREDLVAESPKHLPTMLRYDTYVKNNSLYNTPPSFGIYMVNEVL
KWIEERGGLEGVQQANRKKASLIYDAIDQSGGFYRGCVDVDSRSDMNITF
RLASEELEKEFVKASEQEGFVGLKGHRSVGGLRASIYNAVPYESCEALVQ
FMEHFKRSRG
3D structure
PDB1w3u Enzyme Adaptation to Alkaline Ph: Atomic Resolution (1.08 A) Structure of Phosphoserine Aminotransferase from Bacillus Alcalophilus
ChainA
Resolution1.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) W103 D173 K197
Catalytic site (residue number reindexed from 1) W101 D171 K195
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 G76 A77 S78 W103 T153 D173 S175 Q196 K197 G74 A75 S76 W101 T151 D171 S173 Q194 K195
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:1w3u, PDBe:1w3u, PDBj:1w3u
PDBsum1w3u
PubMed15608117
UniProtQ59196|SERC_NIACI Phosphoserine aminotransferase (Gene Name=serC)

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