Binding Site Information of Target
| Target General Information | Top | ||||
|---|---|---|---|---|---|
| Target ID | T98390 | Target Info | |||
| Target Name | HUMAN angiotensin-converting enzyme 2 (ACE2) | ||||
| Synonyms | Processed angiotensinconverting enzyme 2; Metalloprotease MPROT15; Angiotensinconverting enzyme homolog; Angiotensinconverting enzyme 2; ACErelated carboxypeptidase; ACEH; ACE2 | ||||
| Gene Name | ACE2 | ||||
| Biochemical Class | Peptidase | ||||
| UniProt ID | |||||
| Drug Binding Sites of Target | Top | |||||
|---|---|---|---|---|---|---|
| Ligand Name: ORE-1001 | Ligand Info | |||||
| Structure Description | Inhibitor Bound Human Angiotensin Converting Enzyme-Related Carboxypeptidase (ACE2) | PDB:1R4L | ||||
| Method | X-ray diffraction | Resolution | 3.00 Å | Mutation | No | [1] |
| PDB Sequence |
STIEEQAKTF
28 LDKFNHEAED38 LFYQSSLASW48 NYNTNITEEN58 VQNMNNAGDK68 WSAFLKEQST 78 LAQMYPLQEI88 QNLTVKLQLQ98 ALQQNGSSVL108 SEDKSKRLNT118 ILNTMSTIYS 128 TGKVCNPDNP138 QECLLLEPGL148 NEIMANSLDY158 NERLWAWESW168 RSEVGKQLRP 178 LYEEYVVLKN188 EMARANHYED198 YGDYWRGDYE208 VNGVDGYDYS218 RGQLIEDVEH 228 TFEEIKPLYE238 HLHAYVRAKL248 MNAYPSYISP258 IGCLPAHLLG268 DMWGRFWTNL 278 YSLTVPFGQK288 PNIDVTDAMV298 DQAWDAQRIF308 KEAEKFFVSV318 GLPNMTQGFW 328 ENSMLTDPGN338 VQKAVCHPTA348 WDLGKGDFRI358 LMCTKVTMDD368 FLTAHHEMGH 378 IQYDMAYAAQ388 PFLLRNGANE398 GFHEAVGEIM408 SLSAATPKHL418 KSIGLLSPDF 428 QEDNETEINF438 LLKQALTIVG448 TLPFTYMLEK458 WRWMVFKGEI468 PKDQWMKKWW 478 EMKREIVGVV488 EPVPHDETYC498 DPASLFHVSN508 DYSFIRYYTR518 TLYQFQFQEA 528 LCQAAKHEGP538 LHKCDISNST548 EAGQKLFNML558 RLGKSEPWTL568 ALENVVGAKN 578 MNVRPLLNYF588 EPLFTWLKDQ598 NKNSFVGWST608 DWSPYAD
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GLU145
4.054
ASN149
3.895
ARG273
2.736
PHE274
4.535
CYS344
4.133
HIS345
2.664
PRO346
3.088
THR347
4.034
ALA348
4.946
MET360
3.717
CYS361
4.375
LYS363
4.288
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| Ligand Name: 2-(Acetylamino)-2-Deoxy-a-D-Glucopyranose | Ligand Info | |||||
| Structure Description | Crystal structure of spike protein receptor-binding domain from the 2002-2003 SARS coronavirus human strain complexed with human-civet chimeric receptor ACE2 | PDB:3D0G | ||||
| Method | X-ray diffraction | Resolution | 2.80 Å | Mutation | No | [2] |
| PDB Sequence |
STTEELAKTF
28 LETFNYEAQE38 LSYQSSVASW48 NYNTNITEEN58 VQNMNNAGDK68 WSAFLKEQST 78 LAQMYPLQEI88 QNLTVKLQLQ98 ALQQNGSSVL108 SEDKSKRLNT118 ILNTMSTIYS 128 TGKVCNPDNP138 QECLLLEPGL148 NEIMANSLDY158 NERLWAWESW168 RSEVGKQLRP 178 LYEEYVVLKN188 EMARANHYED198 YGDYWRGDYE208 VNGVDGYDYS218 RGQLIEDVEH 228 TFEEIKPLYE238 HLHAYVRAKL248 MNAYPSYISP258 IGCLPAHLLG268 DMWGRFWTNL 278 YSLTVPFGQK288 PNIDVTDAMV298 DQAWDAQRIF308 KEAEKFFVSV318 GLPNMTQGFW 328 ENSMLTDPGN338 VQKAVCHPTA348 WDLGKGDFRI358 LMCTKVTMDD368 FLTAHHEMGH 378 IQYDMAYAAQ388 PFLLRNGANE398 GFHEAVGEIM408 SLSAATPKHL418 KSIGLLSPDF 428 QEDNETEINF438 LLKQALTIVG448 TLPFTYMLEK458 WRWMVFKGEI468 PKDQWMKKWW 478 EMKREIVGVV488 EPVPHDETYC498 DPASLFHVSN508 DYSFIRYYTR518 TLYQFQFQEA 528 LCQAAKHEGP538 LHKCDISNST548 EAGQKLFNML558 RLGKSEPWTL568 ALENVVGAKN 578 MNVRPLLNYF588 EPLFTWLKDQ598 NKNSFVGWST608 DWSPYAD
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| Click to View More Binding Site Information of This Target and Ligand Pair | ||||||
| Ligand Name: Distearoyl phosphatidic acid | Ligand Info | |||||
| Structure Description | ACE2-B0AT1 complex | PDB:6M18 | ||||
| Method | Electron microscopy | Resolution | 2.90 Å | Mutation | No | [3] |
| PDB Sequence |
TIEEQAKTFL
29 DKFNHEAEDL39 FYQSSLASWN49 YNTNITEENV59 QNMNNAGDKW69 SAFLKEQSTL 79 AQMYPLQEIQ89 NLTVKLQLQA99 LQQNGSSVLS109 EDKSKRLNTI119 LNTMSTIYST 129 GKVCNPDNPQ139 ECLLLEPGLN149 EIMANSLDYN159 ERLWAWESWR169 SEVGKQLRPL 179 YEEYVVLKNE189 MARANHYEDY199 GDYWRGDYEV209 NGVDGYDYSR219 GQLIEDVEHT 229 FEEIKPLYEH239 LHAYVRAKLM249 NAYPSYISPI259 GCLPAHLLGD269 MWGRFWTNLY 279 SLTVPFGQKP289 NIDVTDAMVD299 QAWDAQRIFK309 EAEKFFVSVG319 LPNMTQGFWE 329 NSMLTDPGNV339 QKAVCHPTAW349 DLGKGDFRIL359 MCTKVTMDDF369 LTAHHEMGHI 379 QYDMAYAAQP389 FLLRNGANEG399 FHEAVGEIMS409 LSAATPKHLK419 SIGLLSPDFQ 429 EDNETEINFL439 LKQALTIVGT449 LPFTYMLEKW459 RWMVFKGEIP469 KDQWMKKWWE 479 MKREIVGVVE489 PVPHDETYCD499 PASLFHVSND509 YSFIRYYTRT519 LYQFQFQEAL 529 CQAAKHEGPL539 HKCDISNSTE549 AGQKLFNMLR559 LGKSEPWTLA569 LENVVGAKNM 579 NVRPLLNYFE589 PLFTWLKDQN599 KNSFVGWSTD609 WSPYADQSIK619 VRISLKSALG 629 DKAYEWNDNE639 MYLFRSSVAY649 AMRQYFLKVK659 NQMILFGEED669 VRVANLKPRI 679 SFNFFVTAPK689 NVSDIIPRTE699 VEKAIRMSRS709 RINDAFRLND719 NSLEFLGIQP 729 TLGPPNQPPV739 SIWLIVFGVV749 MGVIVVGIVI759 LIFTGIRDR
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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 .3PH or .3PH2 or .3PH3 or :33PH;style chemicals stick;color identity;select .B:761 or .B:765; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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| References | Top | ||||
|---|---|---|---|---|---|
| REF 1 | ACE2 X-ray structures reveal a large hinge-bending motion important for inhibitor binding and catalysis. J Biol Chem. 2004 Apr 23;279(17):17996-8007. | ||||
| REF 2 | Structural analysis of major species barriers between humans and palm civets for severe acute respiratory syndrome coronavirus infections. J Virol. 2008 Jul;82(14):6984-91. | ||||
| REF 3 | Structural basis for the recognition of SARS-CoV-2 by full-length human ACE2. Science. 2020 Mar 27;367(6485):1444-1448. | ||||
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