Structure of PDB 3meb Chain B

Receptor sequence
>3mebB (length=426) Species: 184922 (Giardia lamblia ATCC 50803) [Search protein sequence]
MSVFSGFPASPPDAILNLTVLYNADTNPKKVNLGVGAYRDESGKPWILPA
VKEAEAIISSDLSKYNKEYPPVAGFPLFLEAAQFLMFGKDSKAAQEGRIA
SCQSLSGTGSLHIGFEFLHLWMPKAEFYMPSTTWPNHYGIYDKVFNKLKV
PYKEYTYLRKDGELEIDFSNTKKDIQSAPEKSIFLFHACAHNPSGIDFTE
AQWKELLPIMKEKKHIAFFDSAYQGFATGSFEADAFAVRMFVDAGVEVLV
AQSFSKNFGLYGERIGCLHVVHAGVEGSVEKNKALSAAMVSGMTLQIRKT
WSMSAIHGAYIVQVIVHDKRLLQMFYDNVKEMSARIHRMRSLLHASLAKR
KTPGPGSKGTWDHILTAIGMFTFTGLTPEHVDYLKEKWSIYLVKAGGRMS
MCGLTESNCDYVAEAIHDAVTKLPFK
3D structure
PDB3meb Structures of aspartate aminotransferases from Trypanosoma brucei, Leishmania major and Giardia lamblia.
ChainB
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) W134 D220 A222 K256
Catalytic site (residue number reindexed from 1) W134 D220 A222 K256
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 B S106 G107 T108 W134 D220 A222 Y223 S253 S255 K256 R264 S106 G107 T108 W134 D220 A222 Y223 S253 S255 K256 R264
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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Cellular Component
External links
PDB RCSB:3meb, PDBe:3meb, PDBj:3meb
PDBsum3meb
PubMed25945710
UniProtA8B1V5

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