Target Information
Target General Information | Top | |||||
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Target ID |
T63159
(Former ID: TTDR00916)
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Target Name |
Plasmodium M1-family aminopeptidase (Malaria MFA)
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Synonyms |
Pfa-M1
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Gene Name |
Malaria MFA
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Target Type |
Literature-reported target
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[1] | ||||
Function |
Displays aminopeptidase activity with a broad substrate specificity. Preferentially hydrolyzes L-Lys-AMC but also shows strong activity against L-Ala-AMC, L-Arg-AMC and L-Leu-AMC.
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BioChemical Class |
Peptidase
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UniProt ID | ||||||
EC Number |
EC 3.4.11.-
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Sequence |
MKLTKGCAYKYIIFTVLILANILYDNKKRCMIKKNLRISSCGIISRLLKSNSNYNSFNKN
YNFTSAISELQFSNFWNLDILQKDIFSNIHNNKNKPQSYIIHKRLMSEKGDNNNNNHQNN NGNDNKKRLGSVVNNEENTCSDKRMKPFEEGHGITQVDKMNNNSDHLQQNGVMNLNSNNV ENNNNNNSVVVKKNEPKIHYRKDYKPSGFIINNVTLNINIHDNETIVRSVLDMDISKHNV GEDLVFDGVGLKINEISINNKKLVEGEEYTYDNEFLTIFSKFVPKSKFAFSSEVIIHPET NYALTGLYKSKNIIVSQCEATGFRRITFFIDRPDMMAKYDVTVTADKEKYPVLLSNGDKV NEFEIPGGRHGARFNDPHLKPCYLFAVVAGDLKHLSATYITKYTKKKVELYVFSEEKYVS KLQWALECLKKSMAFDEDYFGLEYDLSRLNLVAVSDFNVGAMENKGLNIFNANSLLASKK NSIDFSYARILTVVGHEYFHNYTGNRVTLRDWFQLTLKEGLTVHRENLFSEEMTKTVTTR LSHVDLLRSVQFLEDSSPLSHPIRPESYVSMENFYTTTVYDKGSEVMRMYLTILGEEYYK KGFDIYIKKNDGNTATCEDFNYAMEQAYKMKKADNSANLNQYLLWFSQSGTPHVSFKYNY DAEKKQYSIHVNQYTKPDENQKEKKPLFIPISVGLINPENGKEMISQTTLELTKESDTFV FNNIAVKPIPSLFRGFSAPVYIEDNLTDEERILLLKYDSDAFVRYNSCTNIYMKQILMNY NEFLKAKNEKLESFNLTPVNAQFIDAIKYLLEDPHADAGFKSYIVSLPQDRYIINFVSNL DTDVLADTKEYIYKQIGDKLNDVYYKMFKSLEAKADDLTYFNDESHVDFDQMNMRTLRNT LLSLLSKAQYPNILNEIIEHSKSPYPSNWLTSLSVSAYFDKYFELYDKTYKLSKDDELLL QEWLKTVSRSDRKDIYEILKKLENEVLKDSKNPNDIRAVYLPFTNNLRRFHDISGKGYKL IAEVITKTDKFNPMVATQLCEPFKLWNKLDTKRQELMLNEMNTMLQEPNISNNLKEYLLR LTNKL Click to Show/Hide
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3D Structure | Click to Show 3D Structure of This Target | PDB |
Drug Binding Sites of Target | Top | |||||
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Ligand Name: Bestatin | Ligand Info | |||||
Structure Description | Structure of the M1 Alanylaminopeptidase from malaria complexed with bestatin | PDB:3EBH | ||||
Method | X-ray diffraction | Resolution | 1.65 Å | Mutation | Yes | [2] |
PDB Sequence |
PKIHYRKDYK
205 PSGFIINQVT215 LNINIHDQET225 IVRSVLDMDI235 SKHNVGEDLV245 FDGVGLKINE 255 ISINNKKLVE265 GEEYTYDNEF275 LTIFSKFVPK285 SKFAFSSEVI295 IHPETNYALT 305 GLYKSKNIIV315 SQCEATGFRR325 ITFFIDRPDM335 MAKYDVTVTA345 DKEKYPVLLS 355 NGDKVNEFEI365 PGGRHGARFN375 DPPLKPCYLF385 AVVAGDLKHL395 SATYITKYTK 405 KKVELYVFSE415 EKYVSKLQWA425 LECLKKSMAF435 DEDYFGLEYD445 LSRLNLVAVS 455 DFNVGAMENK465 GLNIFNANSL475 LASKKNSIDF485 SYARILTVVG495 HEYFHQYTGN 505 RVTLRDWFQL515 TLKEGLTVHR525 ENLFSEEMTK535 TVTTRLSHVD545 LLRSVQFLED 555 SSPLSHPIRP565 ESYVSMENFY575 TTTVYDKGSE585 VMRMYLTILG595 EEYYKKGFDI 605 YIKKNDGNTA615 TCEDFNYAME625 QAYKMKKADN635 SANLNQYLLW645 FSQSGTPHVS 655 FKYNYDAEKK665 QYSIHVNQYT675 KPDENQKEKK685 PLFIPISVGL695 INPENGKEMI 705 SQTTLELTKE715 SDTFVFNNIA725 VKPIPSLFRG735 FSAPVYIEDQ745 LTDEERILLL 755 KYDSDAFVRY765 NSCTNIYMKQ775 ILMNYNEFLK785 AKNEKLESFQ795 LTPVNAQFID 805 AIKYLLEDPH815 ADAGFKSYIV825 SLPQDRYIIN835 FVSNLDTDVL845 ADTKEYIYKQ 855 IGDKLNDVYY865 KMFKSLEAKA875 DDLTYFNDES885 HVDFDQMNMR895 TLRNTLLSLL 905 SKAQYPNILN915 EIIEHSKSPY925 PSNWLTSLSV935 SAYFDKYFEL945 YDKTYKLSKD 955 DELLLQEWLK965 TVSRSDRKDI975 YEILKKLENE985 VLKDSKNPND995 IRAVYLPFTN 1005 NLRRFHDISG1015 KGYKLIAEVI1025 TKTDKFNPMV1035 ATQLCEPFKL1045 WNKLDTKRQE 1055 LMLNEMNTML1065 QEPQISNNLK1075 EYLLRLTNK
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GLN317
3.826
GLU319
2.711
ALA320
4.261
VAL459
3.202
GLY460
2.546
ALA461
3.032
MET462
3.777
GLU463
2.792
ARG489
4.081
THR492
4.337
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Ligand Name: Arginine | Ligand Info | |||||
Structure Description | A naturally variable residue in the S1 subsite of M1-family aminopeptidases modulates catalytic properties and promotes functional specialization | PDB:4J3B | ||||
Method | X-ray diffraction | Resolution | 2.20 Å | Mutation | Yes | [3] |
PDB Sequence |
KIHYRKDYKP
206 SGFIINNVTL216 NINIHDNETI226 VRSVLDMDIS236 KHNVGEDLVF246 DGVGLKINEI 256 SINNKKLVEG266 EEYTYDNEFL276 TIFSKFVPKS286 KFAFSSEVII296 HPETNYALTG 306 LYKSKNIIVS316 QCEATGFRRI326 TFFIDRPDMM336 AKYDVTVTAD346 KEKYPVLLSN 356 GDKVNEFEIP366 GGRHGARFND376 PHLKPCYLFA386 VVAGDLKHLS396 ATYITKYTKK 406 KVELYVFSEE416 KYVSKLQWAL426 ECLKKSMAFD436 EDYFGLEYDL446 SRLNLVAVSD 456 FNPGAMENKG466 LNIFNANSLL476 ASKKNSIDFS486 YARILTVVGH496 EYFHNYTGNR 506 VTLRDWFQLT516 LKEGLTVHRE526 NLFSEEMTKT536 VTTRLSHVDL546 LRSVQFLEDS 556 SPLSHPIRPE566 SYVSMENFYT576 TTVYDKGSEV586 MRMYLTILGE596 EYYKKGFDIY 606 IKKNDGNTAT616 CEDFNYAMEQ626 AYKMKKADNS636 ANLNQYLLWF646 SQSGTPHVSF 656 KYNYDAEKKQ666 YSIHVNQYTK676 PDENQKEKKP686 LFIPISVGLI696 NPENGKEMIS 706 QTTLELTKES716 DTFVFNNIAV726 KPIPSLFRGF736 SAPVYIEDNL746 TDEERILLLK 756 YDSDAFVRYN766 SCTNIYMKQI776 LMNYNEFLKA786 KNEKLESFNL796 TPVNAQFIDA 806 IKYLLEDPHA816 DAGFKSYIVS826 LPQDRYIINF836 VSNLDTDVLA846 DTKEYIYKQI 856 GDKLNDVYYK866 MFKSLEAKAD876 DLTYFNDESH886 VDFDQMNMRT896 LRNTLLSLLS 906 KAQYPNILNE916 IIEHSKSPYP926 SNWLTSLSVS936 AYFDKYFELY946 DKTYKLSKDD 956 ELLLQEWLKT966 VSRSDRKDIY976 EILKKLENEV986 LKDSKNPNDI996 RAVYLPFTNN 1006 LRRFHDISGK1016 GYKLIAEVIT1026 KTDKFNPMVA1036 TQLCEPFKLW1046 NKLDTKRQEL 1056 MLNEMNTMLQ1066 EPNISNNLKE1076 YLLRLTNK
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Click to View More Binding Site Information of This Target with Different Ligands |
Different Human System Profiles of Target | Top |
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Human Similarity Proteins
of target is determined by comparing the sequence similarity of all human proteins with the target based on BLAST. The similarity proteins for a target are defined as the proteins with E-value < 0.005 and outside the protein families of the target.
A target that has fewer human similarity proteins outside its family is commonly regarded to possess a greater capacity to avoid undesired interactions and thus increase the possibility of finding successful drugs
(Brief Bioinform, 21: 649-662, 2020).
Human Similarity Proteins
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There is no similarity protein (E value < 0.005) for this target
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Chemical Structure based Activity Landscape of Target | Top |
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Target-Related Models and Studies | Top | |||||
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Target Validation |
References | Top | |||||
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REF 1 | In silico identification and biochemical evaluation of novel inhibitors of NRH:quinone oxidoreductase 2 (NQO2). Bioorg Med Chem Lett. 2010 Dec 15;20(24):7331-6. | |||||
REF 2 | Structural basis for the inhibition of the essential Plasmodium falciparum M1 neutral aminopeptidase. Proc Natl Acad Sci U S A. 2009 Feb 24;106(8):2537-42. | |||||
REF 3 | A naturally variable residue in the S1 subsite of M1 family aminopeptidases modulates catalytic properties and promotes functional specialization. J Biol Chem. 2013 Sep 6;288(36):26004-26012. |
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