Structure of PDB 8e9j Chain B

Receptor sequence
>8e9jB (length=399) Species: 562 (Escherichia coli) [Search protein sequence]
HVGTFENITAAPADPILGLADLFRADERPGKINLGIGLYYDETGKIPVLT
SVKKAEQYLLENETTKLYLGIDGIPEFGRCTQELLFGKGSALINDKRART
AQTPGGSGALRVAADFLAKNTSVKRVWVSNPSWPNHKSVFNSAGLEVREY
AYYDAENHTLDFDALINSLNEAQAGDVVLFHGCCHNPTGIDPTLEQWQTL
AQLSVEKGWLPLFDFAYQGFARGLEEDAEGLRAFAAMHKELIVASSYSKN
FGLYNERVGACTLVAADSETVDRAFSQMKAAIRANYSSPPAHGASVVATI
LSNDALRAIWEQELTDMRQRIQRMRQLFVNTLQEKGANRDFSFIIKQNGM
FSFSGLTKEQVLRLREEFGVYAVASGRVNVAGMTPDNMAPLCEAIVAVL
3D structure
PDB8e9j Computational remodeling of an enzyme conformational landscape for altered substrate selectivity.
ChainB
Resolution2.09 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.6.1.1: aspartate 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 G102 G103 S104 W130 D211 A213 Y214 S243 S245 K246 R254 G105 G106 S107 W133 D214 A216 Y217 S246 S248 K249 R257
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004069 L-aspartate:2-oxoglutarate aminotransferase activity
GO:0004838 L-tyrosine-2-oxoglutarate transaminase activity
GO:0008483 transaminase activity
GO:0030170 pyridoxal phosphate binding
GO:0042802 identical protein binding
GO:0042803 protein homodimerization activity
Biological Process
GO:0006520 amino acid metabolic process
GO:0009058 biosynthetic process
GO:0009094 L-phenylalanine biosynthetic process
GO:0033585 L-phenylalanine biosynthetic process from chorismate via phenylpyruvate
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:8e9j, PDBe:8e9j, PDBj:8e9j
PDBsum8e9j
PubMed37770431
UniProtP00509|AAT_ECOLI Aspartate aminotransferase (Gene Name=aspC)

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