Structure of PDB 1cq6 Chain A Binding Site BS01

Receptor Information
>1cq6 Chain A (length=396) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MFENITAAPADPILGLADLFRADERPGKINLGIGVYKDETGKTPVLTSVK
KAEQYLLENETTKNYLGIDGIPEFGRCTQELLFGKGSALINDKRARTAQT
PGGTGALRVAADFLAKNTSVKRVWVSNPSWPNHKSVFNSAGLEVREYAYY
DAENHTLDFDALINSLNEAQAGDVVLFHGCCHNPTGIDPTLEQWQTLAQL
SVEKGWLPLFDFAYQGFARGLEEDAEGLRAFAAMHKELIVASSYSKNFGL
YNERVGACTLVAADSETVDRAFSQMKAAIRANYSNPPAHGASVVATILSN
DALRAIWEQELTDMRQRIQRMRQLFVNTLQEKGANRDFSFIIKQNGMFSF
SGLTKEQVLRLREEFGVYAVASGRVNVAGMTPDNMAPLCEAIVAVL
Ligand information
Ligand IDPY4
InChIInChI=1S/C12H19N2O7P/c1-3-10(12(16)17)14-5-9-8(6-21-22(18,19)20)4-13-7(2)11(9)15/h4,10,14-15H,3,5-6H2,1-2H3,(H,16,17)(H2,18,19,20)/t10-/m1/s1
InChIKeyVRMPGTOTVVJQMU-SNVBAGLBSA-N
SMILES
SoftwareSMILES
CACTVS 3.341CC[C@@H](NCc1c(O)c(C)ncc1CO[P](O)(O)=O)C(O)=O
ACDLabs 10.04O=C(O)C(NCc1c(cnc(c1O)C)COP(=O)(O)O)CC
OpenEye OEToolkits 1.5.0CC[C@H](C(=O)O)NCc1c(cnc(c1O)C)COP(=O)(O)O
CACTVS 3.341CC[CH](NCc1c(O)c(C)ncc1CO[P](O)(O)=O)C(O)=O
OpenEye OEToolkits 1.5.0CCC(C(=O)O)NCc1c(cnc(c1O)C)COP(=O)(O)O
FormulaC12 H19 N2 O7 P
Name2-[O-PHOSPHONOPYRIDOXYL]-AMINO- BUTYRIC ACID;
VITAMIN B6 COMPLEXED WITH 2-AMINO-BUTYRIC ACID
ChEMBL
DrugBank
ZINCZINC000002047163
PDB chain1cq6 Chain A Residue 413 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1cq6 Free energy requirement for domain movement of an enzyme
Resolution2.7 Å
Binding residue
(original residue number in PDB)		G108 T109 W140 N194 D222 Y225 S255 S257 R266
Binding residue
(residue number reindexed from 1)		G103 T104 W130 N183 D211 Y214 S243 S245 R254
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) W140 D222 A224 K258
Catalytic site (residue number reindexed from 1) W130 D211 A213 K246
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:1cq6, PDBe:1cq6, PDBj:1cq6
PDBsum1cq6
PubMed10858450
UniProtP00509|AAT_ECOLI Aspartate aminotransferase (Gene Name=aspC)

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