Structure of PDB 1bkg Chain D

Receptor sequence
>1bkgD (length=382) Species: 300852 (Thermus thermophilus HB8) [Search protein sequence]
MRGLSRRVQAMKPSATVAVNAKALELRRQGVDLVALTAGEPDFDTPEHVK
EAARRALAQGKTKYAPPAGIPELREALAEKFRRENGLSVTPEETIVTVGG
KQALFNLFQAILDPGDEVIVLSPYWVSYPEMVRFAGGVVVEVETLPEEGF
VPDPERVRRAITPRTKALVVNSPNNPTGAVYPKEVLEALARLAVEHDFYL
VSDEIYEHLLYEGEHFSPGRVAPEHTLTVNGAAKAFAMTGWRIGYACGPK
EVIKAMASVSSQSTTSPDTIAQWATLEALTNQEASRAFVEMAREAYRRRR
DLLLEGLTALGLKAVRPSGAFYVLMDTSPIAPDEVRAAERLLEAGVAVVP
GTDFAAFGHVRLSYATSEENLRKALERFARVL
3D structure
PDB1bkg Structure of Thermus thermophilus HB8 aspartate aminotransferase and its complex with maleate.
ChainD
Resolution2.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) W125 D203 I205 K234
Catalytic site (residue number reindexed from 1) W125 D203 I205 K234
Enzyme Commision number 2.6.1.1: aspartate transaminase.
2.6.1.78: aspartate--prephenate aminotransferase.
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 PMP D G99 G100 K101 W125 N171 N175 D203 I205 Y206 K234 R242 G99 G100 K101 W125 N171 N175 D203 I205 Y206 K234 R242
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004069 L-aspartate:2-oxoglutarate aminotransferase activity
GO:0008483 transaminase activity
GO:0030170 pyridoxal phosphate binding
GO:0033853 aspartate-prephenate aminotransferase activity
Biological Process
GO:0006520 amino acid metabolic process
GO:0009058 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:1bkg, PDBe:1bkg, PDBj:1bkg
PDBsum1bkg
PubMed10029535
UniProtQ56232|AAPAT_THET8 Aspartate/prephenate aminotransferase (Gene Name=aspC)

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