Binding Site Information of Target
| Target General Information | Top | ||||
|---|---|---|---|---|---|
| Target ID | T97537 | Target Info | |||
| Target Name | Leucyl-cysteinyl aminopeptidase (LNPEP) | ||||
| Synonyms | Placental leucine aminopeptidase; P-LAP; Oxytocinase; OTase; Leucyl-cystinyl aminopeptidase; Insulin-responsive aminopeptidase; Insulin-regulated membrane aminopeptidase; IRAP; Cystinyl aminopeptidase | ||||
| Target Type | Patented-recorded Target | ||||
| Gene Name | LNPEP | ||||
| Biochemical Class | Peptidase | ||||
| UniProt ID | |||||
| Drug Binding Sites of Target | Top | |||||
|---|---|---|---|---|---|---|
| Ligand Name: L-lysine | Ligand Info | |||||
| Structure Description | Crystal Structure of Human Insulin Regulated Aminopeptidase with Lysine in Active Site | PDB:4PJ6 | ||||
| Method | X-ray diffraction | Resolution | 2.96 Å | Mutation | No | [1] |
| PDB Sequence |
KLFPWAQIRL
168 PTAVVPLRYE178 LSLHPNLTSM188 TFRGSVTISV198 QALQVTWNII208 LHSTGHNISR 218 VTFMSVSSQE229 KQAEILEYAY239 HGQIAIVAPE249 ALLAGHNYTL259 KIEYSANISS 269 SYYGFYGFSY279 TDESNEKKYF289 AATQFEPLAA299 RSAFPCFDEP309 AFKATFIIKI 319 IRDEQYTALS329 NMPKKSSVVL339 DDGLVQDEFS349 ESVKMSTYLV359 AFIVGEMKNL 369 SQDVNGTLVS379 IYAVPEKIGQ389 VHYALETTVK399 LLEFFQNYFE409 IQYPLKKLDL 419 VAIPDFEAGA429 MENWGLLTFR439 EETLLYDSNT449 SSMADRKLVT459 KIIAHELAHQ 469 WFGNLVTMKW479 WNDLWLNEGF489 ATFMEYFSLE499 KIFKELSSYE509 DFLDARFKTM 519 KKDSLNSSHP529 ISSSVQSSEQ539 IEEMFDSLSY549 FKGSSLLLML559 KTYLSEDVFQ 569 HAVVLYLHNH579 SYASIQSDDL589 WDSFNEVTNQ599 TLDVKRMMKT609 WTLQKGFPLV 619 TVQKKGKELF629 IQQERFFLNM639 SDTSYLWHIP655 LSYVTEGRNY665 SKYQSVSLLD 675 KKSGVINLTE685 EVLWVKVNIN695 MNGYYIVHYA705 DDDWEALIHQ715 LKINPYVLSD 725 KDRANLINNI735 FELAGLGKVP745 LKRAFDLINY755 LGNENHTAPI765 TEALFQTDLI 775 YNLLEKLGYM785 DLASRLVTRV795 FKLLQNQIQQ805 QTWTDEGTPS815 MRELRSALLE 825 FACTHNLGNC835 STTAMKLFDD845 WMASNGTQSL855 PTDVMTTVFK865 VGAKTDKGWS 875 FLLGKYISIG885 SEAEKNKILE895 ALASSEDVRK905 LYWLMKSSLN915 GDNFRTQKLS 925 FIIRTVGRHF935 PGHLLAWDFV945 KENWNKLVQK955 FPLGSYTIQN965 IVAGSTYLFS 975 TKTHLSEVQA985 FFENQSEATF995 RLRCVQEALE1005 VIQLNIQWME1015 KNLKSLTWWL 1025
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| Ligand Name: [(2~{s})-2-[[(2~{s})-1-Azanyl-1-Oxidanylidene-3-Phenyl-Propan-2-Yl]carbamoyl]-4,4-Diphenyl-Butyl]-[(1~{r})-1-Azanyl-3-Phenyl-Propyl]phosphinic Acid | Ligand Info | |||||
| Structure Description | Ligand-induced conformational change of Insulin-regulated aminopeptidase: insights on catalytic mechanism and active site plasticity. | PDB:5MJ6 | ||||
| Method | X-ray diffraction | Resolution | 2.53 Å | Mutation | No | [2] |
| PDB Sequence |
NGKLFPWAQI
166 RLPTAVVPLR176 YELSLHPNLT186 SMTFRGSVTI196 SVQALQVTWN206 IILHSTGHNI 216 SRVTFMSAVS226 SQEKQAEILE236 YAYHGQIAIV246 APEALLAGHN256 YTLKIEYSAN 266 ISSSYYGFYG276 FSYTDESNEK286 KYFAATQFEP296 LAARSAFPCF306 DEPAFKATFI 316 IKIIRDEQYT326 ALSNMPKKSS336 VVLDDGLVQD346 EFSESVKMST356 YLVAFIVGEM 366 KNLSQDVNGT376 LVSIYAVPEK386 IGQVHYALET396 TVKLLEFFQN406 YFEIQYPLKK 416 LDLVAIPDFE426 AGAMENWGLL436 TFREETLLYD446 SNTSSMADRK456 LVTKIIAHEL 466 AHQWFGNLVT476 MKWWNDLWLN486 EGFATFMEYF496 SLEKIFKELS506 SYEDFLDARF 516 KTMKKDSLNS526 SHPISSSVQS536 SEQIEEMFDS546 LSYFKGSSLL556 LMLKTYLSED 566 VFQHAVVLYL576 HNHSYASIQS586 DDLWDSFNEV596 TNQTLDVKRM606 MKTWTLQKGF 616 PLVTVQKKGK626 ELFIQQERFF636 LNMSYLWHIP655 LSYVTEGRNY665 SKYQSVSLLD 675 KKSGVINLTE685 EVLWVKVNIN695 MNGYYIVHYA705 DDDWEALIHQ715 LKINPYVLSD 725 KDRANLINNI735 FELAGLGKVP745 LKRAFDLINY755 LGNENHTAPI765 TEALFQTDLI 775 YNLLEKLGYM785 DLASRLVTRV795 FKLLQNQIQQ805 QTWTDEGTPS815 MRELRSALLE 825 FACTHNLGNC835 STTAMKLFDD845 WMASNGTQSL855 PTDVMTTVFK865 VGAKTDKGWS 875 FLLGKYISIG885 SEAEKNKILE895 ALASSEDVRK905 LYWLMKSSLN915 GDNFRTQKLS 925 FIIRTVGRHF935 PGHLLAWDFV945 KENWNKLVQK955 FPLGSYTIQN965 IVAGSTYLFS 975 TKTHLSEVQA985 FFENQSEATF995 RLRCVQEALE1005 VIQLNIQWME1015 KNLKSLTWWL 1025 RTETSQVAPA1035
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GLN293
4.303
GLU295
2.728
PRO296
4.507
GLU426
4.857
ALA427
3.665
GLY428
2.990
ALA429
3.231
MET430
3.883
GLU431
2.741
LEU457
3.309
LYS460
4.100
ILE461
3.515
HIS464
3.254
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| Ligand Name: methyl (2S)-2-[[(2S)-2-[[(2S,3R)-3-azanyl-2-oxidanyl-4-(4-oxidanylphenoxy)butanoyl]amino]-4-methyl-pentanoyl]amino]-3-(1H-indol-3-yl)propanoate | Ligand Info | |||||
| Structure Description | Insulin regulated aminopeptidase (IRAP) in complex with a nanomolar alpha hydroxy beta amino acid based inhibitor. | PDB:7ZYF | ||||
| Method | X-ray diffraction | Resolution | 2.81 Å | Mutation | No | [3] |
| PDB Sequence |
GKLFPWAQIR
167 LPTAVVPLRY177 ELSLHPNLTS187 MTFRGSVTIS197 VQALQVTWNI207 ILHSTGHNIS 217 RVTFMSQEKQ231 AEILEYAYHG241 QIAIVAPEAL251 LAGHNYTLKI261 EYSANISSSY 271 YGFYGFSYTD281 ESNEKKYFAA291 TQFEPLAARS301 AFPCFDEPAF311 KATFIIKIIR 321 DEQYTALSNM331 PKKSSVVLDD341 GLVQDEFSES351 VKMSTYLVAF361 IVGEMKNLSQ 371 DVNGTLVSIY381 AVPEKIGQVH391 YALETTVKLL401 EFFQNYFEIQ411 YPLKKLDLVA 421 IPDFEAGAME431 NWGLLTFREE441 TLLYDSNTSS451 MADRKLVTKI461 IAHELAHQWF 471 GNLVTMKWWN481 DLWLNEGFAT491 FMEYFSLEKI501 FKELSSYEDF511 LDARFKTMKK 521 DSLNSSHPIS531 SSVQSSEQIE541 EMFDSLSYFK551 GSSLLLMLKT561 YLSEDVFQHA 571 VVLYLHNHSY581 ASIQSDDLWD591 SFNEVTTLDV603 KRMMKTWTLQ613 KGFPLVTVQK 623 KGKELFIQQE633 RFFLNSYLWH653 IPLSYVTEGR663 NYSKYQSVSL673 LDKKSGVINL 683 TEEVLWVKVN693 INMNGYYIVH703 YADDDWEALI713 HQLKINPYVL723 SDKDRANLIN 733 NIFELAGLGK743 VPLKRAFDLI753 NYLGNENHTA763 PITEALFQTD773 LIYNLLEKLG 783 YMDLASRLVT793 RVFKLLQNQI803 QQQTWTDEGT813 PSMRELRSAL823 LEFACTHNLG 833 NCSTTAMKLF843 DDWMASNGTQ853 SLPTDVMTTV863 FKVGAKTDKG873 WSFLLGKYIS 883 IGSEAEKNKI893 LEALASSEDV903 RKLYWLMKSS913 LNGDNFRTQK923 LSFIIRTVGR 933 HFPGHLLAWD943 FVKENWNKLV953 QKFPLGSYTI963 QNIVAGSTYL973 FSTKTHLSEV 983 QAFFENQSEA993 TFRLRCVQEA1003 LEVIQLNIQW1013 MEKNLKSLTW1023 WL |
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Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .KFR or .KFR2 or .KFR3 or :3KFR;style chemicals stick;color identity;select .A:272 or .A:293 or .A:295 or .A:296 or .A:426 or .A:427 or .A:428 or .A:429 or .A:430 or .A:431 or .A:457 or .A:460 or .A:461 or .A:464 or .A:465 or .A:468 or .A:487 or .A:494 or .A:541 or .A:544 or .A:549 or .A:960 or .A:961; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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TYR272
2.952
GLN293
3.665
GLU295
2.738
PRO296
3.491
GLU426
3.777
ALA427
3.399
GLY428
2.915
ALA429
3.361
MET430
3.778
GLU431
2.566
LEU457
4.337
LYS460
4.645
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| References | Top | ||||
|---|---|---|---|---|---|
| REF 1 | Crystal structure of human insulin-regulated aminopeptidase with specificity for cyclic peptides. Protein Sci. 2015 Feb;24(2):190-9. | ||||
| REF 2 | Ligand-Induced Conformational Change of Insulin-Regulated Aminopeptidase: Insights on Catalytic Mechanism and Active Site Plasticity. J Med Chem. 2017 Apr 13;60(7):2963-2972. | ||||
| REF 3 | Discovery of Selective Nanomolar Inhibitors for Insulin-Regulated Aminopeptidase Based on Alpha-Hydroxy-beta-amino Acid Derivatives of Bestatin. J Med Chem. 2022 Jul 28;65(14):10098-10117. | ||||
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