Structure of PDB 5nth Chain A

Receptor sequence

>5nthA (length=537) Species: 5664 (Leishmania major)

SAMKRPRSNSIVEETAVSAYVQTCTNFKSNVTFTDISKVSCVAYHVLLVG
ALEQLRDNSLKSVLFYCPAVAEALQRVKAGSTVKTLAEVPGRKGYTEVMV
TALPATTSRTNCPYRADSMSEAVAAACGSVEEGEVLDVYVCAPAGSETAV
ANAVARAAPHSYTAKAGQATKAYMKQAMSLNVVMSSRAAFTQELVRGKSV
CVAELEAICTSVQLCQRLVDTPPCMLDTVVYAEIAAAYAAELGVDMTVIK
GDELREKGYGGIYAVGKCAQYPAHLVTLRYRNPNAAEGAKNIAMVGKGIV
YDCGGLALKPAAHMTNMKTDMGGSAGVFCAFIAVVRSMKMQRTHFSHIAN
ISVTLCLAENAIGPHSYRNDDVVVMKSGKSVEVMNTDAEGRIVLGDGVYY
ATGEQDFVPDVLIDMATLTGAQGVATGSKHAGVYASDAEAEKDMISAGLQ
SGDLCYPVLYCPEYHEEVYKSPCADMRNIANSSSSAGSSCGGYFVEQHLS
ERFRGPFVHVDMAYPTSNTAGATGYGVTLVFEFLRQH

3D structure

• PDB: 5nth Structural Characterization of Acidic M17 Leucine Aminopeptidases from the TriTryps and Evaluation of Their Role in Nutrient Starvation inTrypanosoma brucei.
• Chain: A
• Resolution: 2.5 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): K311 R393
• Catalytic site (residue number reindexed from 1): K309 R391
• Enzyme Commision number: 3.4.11.-

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	BCT	A	A390 E391 G392 R393 L420	A388 E389 G390 R391 L418
BS02	MN	A	K299 D304 D322 E391	K297 D302 D320 E389
BS03	MN	A	D304 D389 E391	D302 D387 E389
BS04	BB2	A	K299 D304 H315 D389 E391 L420	K297 D302 H313 D387 E389 L418

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

External links

• PDB: RCSB:5nth, PDBe:5nth, PDBj:5nth
• PDBsum: 5nth
• PubMed: 28815215
• UniProt: Q4QH17