Structure of PDB 3tat Chain E

Receptor sequence
>3tatE (length=397) Species: 562 (Escherichia coli) [Search protein sequence]
MFQKVDAYAGDPILTLMERFKEDPRSDKVNLSIGLYYNEDGIIPQLQAVA
EAEARLNAQPHGASLYLPMEGLNCYRHAIAPLLFGADHPVLKQQRVATIQ
TLGGSGALKVGADFLKRYFPESGVWVSDPTWENHVAIFAGAGFEVSTYPW
YDEATNGVRFNDLLATLKTLPARSIVLLHPCCHNPTGADLTNDQWDAVIE
ILKARELIPFLDIAYQGFGAGMEEDAYAIRAIASAGLPALVSNSFSKIFS
LYGERVGGLSVMCEDAEAAGRVLGQLKATVRRNYSSPPNFGAQVVAAVLN
DEALKASWLAEVEEMRTRILAMRQELVKVLSTEMPERNFDYLLNQRGMFS
YTGLSAAQVDRLREEFGVYLIASGRMCVAGLNTANVQRVAKAFAAVM
3D structure
PDB3tat Crystallization and preliminary crystallographic analysis of the Escherichia coli tyrosine aminotransferase.
ChainE
Resolution3.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
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 PLP E G107 G108 S109 H189 N194 A224 S257 K258 R266 G103 G104 S105 H179 N184 A214 S246 K247 R255
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:3tat, PDBe:3tat, PDBj:3tat
PDBsum3tat
PubMed10417420
UniProtP04693|TYRB_ECOLI Aromatic-amino-acid aminotransferase (Gene Name=tyrB)

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