Structure of PDB 4x2t Chain G

Receptor sequence
>4x2tG (length=519) Species: 36329 (Plasmodium falciparum 3D7) [Search protein sequence]
ASEVPQVVSLDPTSIPIEYNTPIHDIKVQVYDIKGGCNVEEGLTIFLVNN
PGKENGPVKISSKVNDKQVSEFLKDENMEKFNVKLGTSKHFYMFNDNKNS
VAVGYVGCGSVADLSEADMKRVVLSLVTMLHDNKLSKLTVVFEINVDKNL
FRFFLETLFYEYMTDERFKSTDKNVNMEYIKHLGVYINNADTYKEEVEKA
RVYYFGTYYASQLIAAPSNYCNPVSLSNAAVELAQKLNLEYKILGVKELE
ELKMGAYLSVGKGSMYPNKFIHLTYKSKGDVKKKIALVGKGITFDSGGYN
LKAAPGSMIDLMKFDMSGCAAVLGCAYCVGTLKPENVEIHFLSAVCENMV
SKNSYRPGDIITASNGKTIEVGNTDAEGRLTLADALVYAEKLGVDYIVDI
ATLTGAMLYSLGTSYAGVFGNNEELINKILQSSKTSNEPVWWLPIINEYR
ATLNSKYADINQISSSVKASSIVASLFLKEFVQNTAWAHIDIAGVSWNFK
ARKPKGFGVRLLTEFVLND
3D structure
PDB4x2t X-ray crystal structures of an orally available aminopeptidase inhibitor, Tosedostat, bound to anti-malarial drug targets PfA-M1 and PfA-M17.
ChainG
Resolution2.729 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K386 R463
Catalytic site (residue number reindexed from 1) K302 R379
Enzyme Commision number 3.4.11.1: leucyl aminopeptidase.
3.4.13.-
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 ZN G D379 D459 E461 D295 D375 E377
BS02 ZN G K374 D379 D399 E461 K290 D295 D315 E377
BS03 TOD G D379 K386 D459 E461 G489 D295 K302 D375 E377 G405
BS04 CO3 G A460 E461 G462 R463 L487 A376 E377 G378 R379 L403
Gene Ontology
Molecular Function
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:4x2t, PDBe:4x2t, PDBj:4x2t
PDBsum4x2t
PubMed25645579
UniProtQ8IL11|AMPL_PLAF7 Leucine aminopeptidase (Gene Name=LAP)

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