PDB 6f5v

PDB Information

PDB6F5V
MethodX-RAY DIFFRACTION
Host OrganismEscherichia coli
Gene SourceArabidopsis thaliana
Primary Citation
Tyrosine metabolism: identification of a key residue in the acquisition of prephenate aminotransferase activity by 1 beta aspartate aminotransferase.
Giustini, C., Graindorge, M., Cobessi, D., Crouzy, S., Robin, A., Curien, G., Matringe, M.
Febs J.
HeaderTransferase
Released2017-12-03
Resolution1.700
CATH Insert Date17 Mar, 2019

PDB Images (13)

PDB Prints

PDB Chains (4)

Chain ID Date inserted into CATH CATH Status
A 17 Mar, 2019 Chopped
B 17 Mar, 2019 Chopped
C 17 Mar, 2019 Chopped
D 17 Mar, 2019 Chopped

CATH Domains (8)

Domain ID Date inserted into CATH Superfamily CATH Status
6f5vA01 18 Mar, 2019 3.90.1150.10 Assigned
6f5vA02 18 Mar, 2019 3.40.640.10 Assigned
6f5vB01 18 Mar, 2019 3.90.1150.10 Assigned
6f5vB02 18 Mar, 2019 3.40.640.10 Assigned
6f5vC01 18 Mar, 2019 3.90.1150.10 Assigned
6f5vC02 18 Mar, 2019 3.40.640.10 Assigned
6f5vD01 18 Mar, 2019 3.90.1150.10 Assigned
6f5vD02 18 Mar, 2019 3.40.640.10 Assigned

UniProtKB Entries (4)

Accession Gene ID Taxon Description
Q9SIE1 PAT_ARATH Arabidopsis thaliana Bifunctional aspartate aminotransferase and glutamate/aspartate-prephenate aminotransferase
Q9SIE1 PAT_ARATH Arabidopsis thaliana Bifunctional aspartate aminotransferase and glutamate/aspartate-prephenate aminotransferase
Q9SIE1 PAT_ARATH Arabidopsis thaliana Bifunctional aspartate aminotransferase and glutamate/aspartate-prephenate aminotransferase
Q9SIE1 PAT_ARATH Arabidopsis thaliana Bifunctional aspartate aminotransferase and glutamate/aspartate-prephenate aminotransferase
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