Structure of PDB 3ihj Chain A

Receptor sequence
>3ihjA (length=461) Species: 9606 (Homo sapiens) [Search protein sequence]
NLYFQSMTLESMNPQVKAVEYAVRGPIVLKAGEIELELQRGIKKPFTEVI
RANPITFLRQVMALCTYPNLLDSPSFPEDAKKRARRILQACSQGVNCIRE
DVAAYITRRDGGVPADPDNIYLTTGASDGISTILKILVSGGGKSRTGVMI
PIPQYPLYSAVISELDAIQVNYYLDEENCWALNVNELRRAVQEAKDHCDP
KVLCIINPGNPTGQVQSRKCIEDVIHFAWEEKLFLLADEVYQDNVYSPDC
RFHSFKKVLYEMGPEYSSNVELASFHSTSKGYMGECGYRGGYMEVINLHP
EIKGQLVKLLSVRLCPPVSGQAAMDIVVNPPVAGEESFEQFSREKESVLG
NLAKKAKLTEDLFNQVPGIHCNPLQGAMYAFPRIFIPAKAVEAAQAHQMA
PDMFYCMKLLEETGICVVPGSGFGQREGTYHFRMTILPPVEKLKTVLQKV
KDFHINFLEKY
3D structure
PDB3ihj Human glutamate pyruvate transaminase 2
ChainA
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) Y216 D299 V301 K341
Catalytic site (residue number reindexed from 1) Y155 D238 V240 K280
Enzyme Commision number 2.6.1.2: alanine 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 A G186 A187 S188 Y216 D299 V301 S338 K341 R350 G125 A126 S127 Y155 D238 V240 S277 K280 R289
Gene Ontology
Molecular Function
GO:0004021 L-alanine:2-oxoglutarate aminotransferase activity
GO:0008483 transaminase activity
GO:0030170 pyridoxal phosphate binding
Biological Process
GO:0006103 2-oxoglutarate metabolic process
GO:0009058 biosynthetic process
GO:0042851 L-alanine metabolic process
GO:0042853 L-alanine catabolic process
Cellular Component
GO:0005739 mitochondrion
GO:0005759 mitochondrial matrix

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3ihj, PDBe:3ihj, PDBj:3ihj
PDBsum3ihj
PubMed
UniProtQ8TD30|ALAT2_HUMAN Alanine aminotransferase 2 (Gene Name=GPT2)

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