Structure of PDB 2bie Chain B Binding Site BS03
Receptor Information
>2bie Chain B (length=355) Species:
1445
(Alkalihalobacillus alcalophilus) [
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QVFNFNAGPSALPKPALERAQKELLNFNDTQMSVMELSHRSQSYEEVHEQ
AQNLLRELLQIPNDYQILFLQGGASLQFTMLPMNLLTKGTIGNYVLTGSW
SEKALKEAKLLGETHIAASTKANSYQSIPDFSEFQLNENDAYLHITSNNT
IYGTQYQNFPEINHAPLIADMSSDILSRPLKVNQFGMIYAGAQKNLGPSG
VTVVIVKKDLLVEQVPTMLQYATHIKSDSLYNTPPTFSIYMLRNVLDWIK
DLGGAEAIAKQNEEKAKIIYDTIDESNGFYVGHAEKGSRSLMNVTFNLRN
EELNQQFLAKAKEQGFVGLNGHRSVGGCRASIYNAVPIDACIALRELMIQ
FKENA
Ligand information
Ligand ID
MG
InChI
InChI=1S/Mg/q+2
InChIKey
JLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mg+2]
CACTVS 3.341
[Mg++]
Formula
Mg
Name
MAGNESIUM ION
ChEMBL
DrugBank
DB01378
ZINC
PDB chain
2bie Chain B Residue 1364 [
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Receptor-Ligand Complex Structure
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PDB
2bie
Strain Relief at the Active Site of Phosphoserine Aminotransferase Induced by Radiation Damage.
Resolution
1.3 Å
Binding residue
(original residue number in PDB)
Y127 Y154 H288
Binding residue
(residue number reindexed from 1)
Y125 Y152 H283
Annotation score
1
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.
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:2bie
,
PDBe:2bie
,
PDBj:2bie
PDBsum
2bie
PubMed
15883191
UniProt
Q9RME2
|SERC_ALKAL Phosphoserine aminotransferase (Gene Name=serC)
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