Structure of PDB 4azj Chain B

Receptor sequence
>4azjB (length=358) Species: 1445 (Alkalihalobacillus alcalophilus) [Search protein sequence]
QVFNFNAGPSALPKPALERAQKELLNFNDTQMSVMELSHRSQSYEEVHEQ
AQNLLRELLQIPNDYQILFLQGGASLQFTMLPMNLLTKGTIGNYVLTGSW
SEKALKEAKLLGETHIAASTKANSYQSIPDFSEFQLNENDAYLHITSNNT
IYGTQYQNFPEINHAPLIADMSSDILSRPLKVNQFGMIYAGAQKNLGPSG
VTVVIVKKDLLNTKVEQVPTMLQYATHIKSDSLYNTPPTFSIYMLRNVLD
WIKDLGGAEAIAKQNEEKAKIIYDTIDESNGFYVGHAEKGSRSLMNVTFN
LRNEELNQQFLAKAKEQGFVGLNGHRSVGGCRASIYNAVPIDACIALREL
MIQFKENA
3D structure
PDB4azj Structural Basis of L-Phosphoserine Binding to Bacillus Alcalophilus Phosphoserine Aminotransferase
ChainB
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) 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 SEP B H41 R42 H39 R40
BS02 PLP B N237 T238 N235 T236
BS03 SEP B W102 T152 K196 H327 R328 R334 W100 T150 K194 H325 R326 R332
BS04 PLP B A76 S77 W102 T152 D172 S174 Q195 K196 A74 S75 W100 T150 D170 S172 Q193 K194
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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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:4azj, PDBe:4azj, PDBj:4azj
PDBsum4azj
PubMed23633589
UniProtQ9RME2|SERC_ALKAL Phosphoserine aminotransferase (Gene Name=serC)

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