Structure of PDB 5ntg Chain B

Receptor sequence
>5ntgB (length=510) Species: 5693 (Trypanosoma cruzi) [Search protein sequence]
GASEFVRSCVNFETNVEFTDVDAYKKTHTAGLASTFVVILGTHAQLREDA
LKELPFYCPAVAEAIQRVKKGETYAVLAEGVKNEANERFVRVLVGEVPSE
ASRTNCPARPDVVASLLSAALEEIKGPETKVDVFVRSTAALAIAVAAARS
AKRNFTAKEGLATRGYCDNCVRLTVVFPTAPNPSPSELAVVATSTQLCQR
LVDAPTNLLNTATFAEVAQSYAKELGCAVDVICGEELRERGYGGIYSVGK
CAVEAPRLVTLSYKPKDETRKKVALVGKGIVYDSGGLSLKPTNFMTGMKR
DMGGAAAVFCGFLTAVRLQMPIELSCTLCLAENAIGPDAYRNDDILTLKS
GKTVEVNNTDAEGRLVLGDGVFHATHEISFKPDVLVDMATLTGAQGIATG
HRHAGIFVNDEEEELSFLKAGRASGETCFPVLYCPEYHVTEFRSPVADMR
NSVKQVNNASVSCAGQFVANHLSPDFKGKHIHVDMAFPAFENDKATGFGP
ALLTEYLRNL
3D structure
PDB5ntg Structural Characterization of Acidic M17 Leucine Aminopeptidases from the TriTryps and Evaluation of Their Role in Nutrient Starvation inTrypanosoma brucei.
ChainB
Resolution2.32 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K300 R374
Catalytic site (residue number reindexed from 1) K290 R364
Enzyme Commision number ?
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 MN B D293 K300 D370 E372 D283 K290 D360 E362
Gene Ontology
Molecular Function
GO:0004177 aminopeptidase activity
GO:0008233 peptidase activity
GO:0030145 manganese ion binding
GO:0046872 metal ion binding
GO:0070006 metalloaminopeptidase activity
Biological Process
GO:0006508 proteolysis
GO:0019538 protein metabolic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5ntg, PDBe:5ntg, PDBj:5ntg
PDBsum5ntg
PubMed28815215
UniProtV5BWE3

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