Structure of PDB 3k7y Chain A

Receptor sequence
>3k7yA (length=405) Species: 36329 (Plasmodium falciparum 3D7) [Search protein sequence]
MDKLLSSLENIEVDNILKTAREFKEDTCEEKINLSIGVCCNDDGDLHIFD
SVLNADKLVTENYKEKPYLLGNGTEDFSTLTQNLIFGNNSKYIEDKKICT
IQCIGGTGAIFVLLEFLKMLNVETLYVTNPPYINHVNMIESRGFNLKYIN
FFDYNLIDINYDLFLNDLRNIPNGSSVILQISCYNPCSVNIEEKYFDEII
EIVLHKKHVIIFDIAYQGFGHTNLEEDVLLIRKFEEKNIAFSVCQSFSKN
MSLYGERAGALHIVCKNQEEKKIVFNNLCFIVRKFYSSPVIHTNRILCQL
LNNQNLKLNWIKELSQLSQRITNNRILFFNKLETYQKKYNLNYDWNVYKK
QRGLFSFVPLLAKIAEHLKTHHIYIINNGRINVSGITKNNVDYIADKICL
SLSQI
3D structure
PDB3k7y Specific Inhibition of the Aspartate Aminotransferase of Plasmodium falciparum.
ChainA
Resolution2.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y132 D213 A215 K249
Catalytic site (residue number reindexed from 1) Y132 D213 A215 K249
Enzyme Commision number 2.6.1.1: aspartate 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 G105 G106 T107 Y132 Q180 D213 A215 Y216 S246 S248 K249 R257 G105 G106 T107 Y132 Q180 D213 A215 Y216 S246 S248 K249 R257
BS02 ACT A N330 K349 N330 K349
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004069 L-aspartate:2-oxoglutarate aminotransferase activity
GO:0008483 transaminase activity
GO:0030170 pyridoxal phosphate binding
Biological Process
GO:0006520 amino acid metabolic process
GO:0009058 biosynthetic process
Cellular Component
GO:0005739 mitochondrion

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3k7y, PDBe:3k7y, PDBj:3k7y
PDBsum3k7y
PubMed21087616
UniProtO96142

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