Structure of PDB 3dyd Chain B

Receptor sequence
>3dydB (length=387) Species: 9606 (Homo sapiens) [Search protein sequence]
WSVRPSDVKPNPNKTMISLSIGDPTVFGNLPTDPEVTQAMKDALDSGKYN
GYAPSIGFLSSREEIASYYHCPEAPLEAKDVILTSGCSQAIDLCLAVLAN
PGQNILVPRPGFSLYKTLAESMGIEVKLYNLLPEKSWEIDLKQLEYLIDE
KTACLIVNNPSNPCGSVFSKRHLQKILAVAARQCVPILADEIYGDMVFSD
CKYEPLATLSTDVPILSCGGLAKRWLVPGWRLGWILIHDRRDIFGNEIRD
GLVKLSQRILGPCTIVQGALKSILCRTPGEFYHNTLSFLKSNADLCYGAL
AAIPGLRPVRPSGAMYLMVGIEMEHFPEFENDVEFTERLVAEQSVHCLPA
TCFEYPNFIRVVITVPEVMMLEACSRIQEFCEQHYHC
3D structure
PDB3dyd Human Tyrosine Aminotransferase
ChainB
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) F169 D247 I249
Catalytic site (residue number reindexed from 1) F112 D190 I192
Enzyme Commision number 2.6.1.5: tyrosine 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 B C144 S145 F169 N219 D247 I249 Y250 A279 K280 R288 C87 S88 F112 N162 D190 I192 Y193 A222 K223 R231
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004838 L-tyrosine-2-oxoglutarate transaminase activity
GO:0008483 transaminase activity
GO:0030170 pyridoxal phosphate binding
Biological Process
GO:0006520 amino acid metabolic process
GO:0009058 biosynthetic process
GO:0009072 aromatic amino acid metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3dyd, PDBe:3dyd, PDBj:3dyd
PDBsum3dyd
PubMed
UniProtP17735|ATTY_HUMAN Tyrosine aminotransferase (Gene Name=TAT)

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