Structure of PDB 4r7m Chain C

Receptor sequence
>4r7mC (length=518) Species: 36329 (Plasmodium falciparum 3D7) [Search protein sequence]
SEVPQVVSLDPTSIPIEYNTPIHDIKVQVYDIKGGCNVEEGLTIFLVNNP
GKENGPVKISSKVNDKQVSEFLKDENMEKFNVKLGTSKHFYMFNDNKNSV
AVGYVGCGSVADLSEADMKRVVLSLVTMLHDNKLSKLTVVFEINVDKNLF
RFFLETLFYEYMTDERFKSTDKNVNMEYIKHLGVYINNADTYKEEVEKAR
VYYFGTYYASQLIAAPSNYCNPVSLSNAAVELAQKLNLEYKILGVKELEE
LKMGAYLSVGKGSMYPNKFIHLTYKSKGDVKKKIALVGKGITFDSGGYNL
KAAPGSMIDLMKFDMSGCAAVLGCAYCVGTLKPENVEIHFLSAVCENMVS
KNSYRPGDIITASNGKTIEVGNTDAEGRLTLADALVYAEKLGVDYIVDIA
TLTGAMLYSLGTSYAGVFGNNEELINKILQSSKTSNEPVWWLPIINEYRA
TLNSKYADINQISSSVKASSIVASLFLKEFVQNTAWAHIDIAGVSWNFKA
RKPKGFGVRLLTEFVLND
3D structure
PDB4r7m Two-Pronged Attack: Dual Inhibition of Plasmodium falciparum M1 and M17 Metalloaminopeptidases by a Novel Series of Hydroxamic Acid-Based Inhibitors.
ChainC
Resolution2.85 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) K301 R378
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 C K374 D379 D399 E461 K289 D294 D314 E376
BS02 CO3 C G462 R463 L487 G377 R378 L402
BS03 ZN C D379 D459 E461 D294 D374 E376
BS04 3MW C K374 D379 K386 D459 E461 L487 T488 G489 L492 A577 K289 D294 K301 D374 E376 L402 T403 G404 L407 A492 BindingDB: Ki=0.011000nM
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:4r7m, PDBe:4r7m, PDBj:4r7m
PDBsum4r7m
PubMed25299353
UniProtQ8IL11|AMPL_PLAF7 Leucine aminopeptidase (Gene Name=LAP)

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