Structure of PDB 2qb2 Chain A Binding Site BS01

Receptor Information
>2qb2 Chain A (length=383) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MFENITAAPDLFRAKINLGIGVYKDETGKTPVLTSVKKAEQYLLENETTK
NYLGIDGIPEFGRCTQELLFGKGSALINDKRARTAQTPGGTGALRVAADF
LAKNTSVKRVWVSNPSWPNHKSVFNSAGLEVREYAYYDAENHTLDFDALI
NSLNEAQAGDVVLFHGCCHNPTGIDPTLEQWQTLAQLSVEKGWLPLFDFA
YQGFARGLEEDAEGLRAFAAMHKELIVASSYSKNFGLYNERVGACTLVAA
DSETVDRAFSQMKAAIRANYSNPPAHGASVVATILSNDALRAIWEQELTD
MRQRIQRMRQLFVNTLQEKGANRDFSFIIKQNGMFSFSGLTKEQVLRLRE
EFGVYAVASGRVNVAGMTPDNMAPLCEAIVAVL
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 chain2qb2 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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PDB2qb2 Inactivation of Escherichia coli L-aspartate aminotransferase by (S)-4-amino-4,5-dihydro-2-thiophenecarboxylic acid reveals "a tale of two mechanisms".
Resolution1.7 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)		G21 G90 T91 W117 N170 D198 A200 Y201 S230 S232 X233 R241 F335 R361
Annotation score1
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.
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:2qb2, PDBe:2qb2, PDBj:2qb2
PDBsum2qb2
PubMed17713924
UniProtP00509|AAT_ECOLI Aspartate aminotransferase (Gene Name=aspC)

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