Structure of PDB 2qb2 Chain A

Receptor sequence
>2qb2A (length=383) Species: 562 (Escherichia coli) [Search protein sequence]
MFENITAAPDLFRAKINLGIGVYKDETGKTPVLTSVKKAEQYLLENETTK
NYLGIDGIPEFGRCTQELLFGKGSALINDKRARTAQTPGGTGALRVAADF
LAKNTSVKRVWVSNPSWPNHKSVFNSAGLEVREYAYYDAENHTLDFDALI
NSLNEAQAGDVVLFHGCCHNPTGIDPTLEQWQTLAQLSVEKGWLPLFDFA
YQGFARGLEEDAEGLRAFAAMHKELIVASSYSKNFGLYNERVGACTLVAA
DSETVDRAFSQMKAAIRANYSNPPAHGASVVATILSNDALRAIWEQELTD
MRQRIQRMRQLFVNTLQEKGANRDFSFIIKQNGMFSFSGLTKEQVLRLRE
EFGVYAVASGRVNVAGMTPDNMAPLCEAIVAVL
3D structure
PDB2qb2 Inactivation of Escherichia coli L-aspartate aminotransferase by (S)-4-amino-4,5-dihydro-2-thiophenecarboxylic acid reveals "a tale of two mechanisms".
ChainA
Resolution1.7 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) W130 D211 A213 K246
Catalytic site (residue number reindexed from 1) W117 D198 A200 K233
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 PSZ A G34 G103 T104 W130 N183 D211 A213 Y214 S243 S245 X246 R254 F348 R374 G21 G90 T91 W117 N170 D198 A200 Y201 S230 S232 X233 R241 F335 R361
BS02 PMP A G103 T104 W130 D211 A213 Y214 S243 S245 X246 R254 G90 T91 W117 D198 A200 Y201 S230 S232 X233 R241
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

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:2qb2, PDBe:2qb2, PDBj:2qb2
PDBsum2qb2
PubMed17713924
UniProtP00509|AAT_ECOLI Aspartate aminotransferase (Gene Name=aspC)

[Back to BioLiP]