Structure of PDB 2qa3 Chain A Binding Site BS01

Receptor Information
>2qa3 Chain A (length=385) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MFENITAAPAADLFRADINLGIGVYKDETGKTPVLTSVKKAEQYLLENET
TKNYLGIDGIPEFGRCTQELLFGKGSALINDKRARTAQTPGGTGALRVAA
DFLAKNTSVKRVWVSNPSWPNHKSVFNSAGLEVREYAYYDAENHTLDFDA
LINSLNEAQAGDVVLFHGCCHNPTGIDPTLEQWQTLAQLSVEKGWLPLFD
FAYQGFARGLEEDAEGLRAFAAMHKELIVASSYSKNFGLYNERVGACTLV
AADSETVDRAFSQMKAAIRANYSNPPAHGASVVATILSNDALRAIWEQEL
TDMRQRIQRMRQLFVNTLQEKGANRDFSFIIKQNGMFSFSGLTKEQVLRL
REEFGVYAVASGRVNVAGMTPDNMAPLCEAIVAVL
Ligand information
Ligand IDPSZ
InChIInChI=1S/C13H15N2O7PS/c1-7-12(16)10(8(3-14-7)5-22-23(19,20)21)4-15-9-2-11(13(17)18)24-6-9/h2-3,6,15-16H,4-5H2,1H3,(H,17,18)(H2,19,20,21)
InChIKeySUKBSASAEROGCJ-UHFFFAOYSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0Cc1c(c(c(cn1)COP(=O)(O)O)CNc2cc(sc2)C(=O)O)O
CACTVS 3.341Cc1ncc(CO[P](O)(O)=O)c(CNc2csc(c2)C(O)=O)c1O
ACDLabs 10.04O=P(O)(O)OCc1c(c(O)c(nc1)C)CNc2cc(sc2)C(=O)O
FormulaC13 H15 N2 O7 P S
Name4-[({3-HYDROXY-2-METHYL-5-[(PHOSPHONOOXY)METHYL]PYRIDIN-4-YL}METHYL)AMINO]THIOPHENE-2-CARBOXYLIC ACID
ChEMBL
DrugBank
ZINCZINC000034553600
PDB chain2qa3 Chain A Residue 600 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2qa3 Inactivation of Escherichia coli L-aspartate aminotransferase by (S)-4-amino-4,5-dihydro-2-thiophenecarboxylic acid reveals "a tale of two mechanisms".
Resolution1.75 Å
Binding residue
(original residue number in PDB)		G34 G103 T104 W130 N183 D211 A213 Y214 S243 S245 X246 R254 F348 R374
Binding residue
(residue number reindexed from 1)		G23 G92 T93 W119 N172 D200 A202 Y203 S232 S234 X235 R243 F337 R363
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) W130 D211 A213 K246
Catalytic site (residue number reindexed from 1) W119 D200 A202 K235
Enzyme Commision number 2.6.1.1: aspartate transaminase.
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:2qa3, PDBe:2qa3, PDBj:2qa3
PDBsum2qa3
PubMed17713924
UniProtP00509|AAT_ECOLI Aspartate aminotransferase (Gene Name=aspC)

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