Structure of PDB 3fsl Chain C Binding Site BS01

Receptor Information
>3fsl Chain C (length=397) Species: 83333 (Escherichia coli K-12) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MFQKVDAYAGDPILTLMERFKEDPRSDKVNLSIGLYYNEDGIIPQLQAVA
EAEARLNAQPHGASLYLPMEGLNCYRHAIAPLLFGADHPVLKQQRVATIQ
TLGGSGALKVGADFLKRYFPESGVWVSDPTWENHVAIFAGAGFEVSTYPW
YDEATNGVRFNDLLATLKTLQAGSIVLLHPCCHNPTGADLTNDQWDAVIE
ILKARELIPFLDIAYQGFGAGMEEDAYAIRAIASAGLPALVSNSFSKIFS
LYGERVGGLSVMCEDAEAAGRVLGQLKATVRRNYSSPPNFGAQVVAAVLN
DEALKASWLKEVEEMRTRILAMRQELVKVLSTEMPERNFDYLLNQRGMFS
YTGLSAAQVDRLREEFGVYLIASGRMCVAGLNTANVQRVAKAFAAVM
Ligand information
Ligand IDPLR
InChIInChI=1S/C8H12NO5P/c1-5-7(4-14-15(11,12)13)3-9-6(2)8(5)10/h3,10H,4H2,1-2H3,(H2,11,12,13)
InChIKeyRBCOYOYDYNXAFA-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341Cc1ncc(CO[P](O)(O)=O)c(C)c1O
ACDLabs 10.04O=P(O)(O)OCc1cnc(c(O)c1C)C
OpenEye OEToolkits 1.5.0Cc1c(cnc(c1O)C)COP(=O)(O)O
FormulaC8 H12 N O5 P
Name(5-HYDROXY-4,6-DIMETHYLPYRIDIN-3-YL)METHYL DIHYDROGEN PHOSPHATE;
4'-DEOXYPYRIDOXINE PHOSPHATE
ChEMBLCHEMBL1235333
DrugBank
ZINCZINC000001656021
PDB chain3fsl Chain C Residue 500 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB3fsl Crystal structure of tyrosine aminotransferase tripple mutant (P181Q,R183G,A321K) from Escherichia coli at 2.35 A resolution
Resolution2.35 Å
Binding residue
(original residue number in PDB)		G107 G108 S109 W140 N194 D222 A224 Y225 S255 S257 K258 R266
Binding residue
(residue number reindexed from 1)		G103 G104 S105 W131 N184 D212 A214 Y215 S244 S246 K247 R255
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) W140 D222 A224 K258
Catalytic site (residue number reindexed from 1) W131 D212 A214 K247
Enzyme Commision number 2.6.1.107: beta-methylphenylalanine transaminase.
2.6.1.57: aromatic-amino-acid transaminase.
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004838 L-tyrosine-2-oxoglutarate transaminase activity
GO:0008483 transaminase activity
GO:0008793 aromatic-amino-acid transaminase activity
GO:0030170 pyridoxal phosphate binding
GO:0042802 identical protein binding
GO:0042803 protein homodimerization activity
GO:0080130 L-phenylalanine-2-oxoglutarate transaminase activity
Biological Process
GO:0006520 amino acid metabolic process
GO:0006532 aspartate biosynthetic process
GO:0006571 tyrosine biosynthetic process
GO:0008652 amino acid biosynthetic process
GO:0009058 biosynthetic process
GO:0009073 aromatic amino acid family biosynthetic process
GO:0009094 L-phenylalanine biosynthetic process
GO:0009098 L-leucine biosynthetic process
GO:0019292 L-tyrosine biosynthetic process from chorismate via 4-hydroxyphenylpyruvate
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:3fsl, PDBe:3fsl, PDBj:3fsl
PDBsum3fsl
PubMed
UniProtP04693|TYRB_ECOLI Aromatic-amino-acid aminotransferase (Gene Name=tyrB)

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