Target Binding Site Detail
| Target General Information | Top | ||||
|---|---|---|---|---|---|
| Target ID | T98311 | Target Info | |||
| Target Name | HUMAN angiotensin-converting enzyme (ACE) | ||||
| Synonyms | Kininase II; Dipeptidyl carboxypeptidase I; DCP1; DCP; CD143 antigen; CD143; ACE | ||||
| Gene Name | SLC33A1 | ||||
| Biochemical Class | Glycosylase | ||||
| UniProt ID | |||||
| Ligand General Information | Top | ||||
|---|---|---|---|---|---|
| Ligand Name | (2~{S})-1-[(2~{S})-2-[[(1~{S})-1-[(2~{S})-1-[(2~{S})-2-azanyl-4-oxidanyl-4-oxidanylidene-butanoyl]pyrrolidin-2-yl]-2-oxidanyl-2-oxidanylidene-ethyl]amino]propanoyl]pyrrolidine-2-carboxylic acid | Ligand Info | |||
| Canonical SMILES | CC(C(=O)N1CCCC1C(=O)O)NC(C2CCCN2C(=O)C(CC(=O)O)N)C(=O)O | ||||
| InChI | 1S/C18H28N4O8/c1-9(15(25)22-7-3-5-12(22)17(27)28)20-14(18(29)30)11-4-2-6-21(11)16(26)10(19)8-13(23)24/h9-12,14,20H,2-8,19H2,1H3,(H,23,24)(H,27,28)(H,29,30)/t9-,10-,11-,12-,14-/m0/s1 | ||||
| InChIKey | AEFOOLCGQAWEBH-JNLQPACOSA-N | ||||
| PubChem Compound ID | 131953530 | ||||
| Drug Binding Sites of Target | Top | |||||
|---|---|---|---|---|---|---|
| PDB ID: 6TT3 Crystal structure of 'Res_S2 mutant human Angiotensin-1 converting enzyme N-domain in complex with SG6. | ||||||
| Method | X-ray diffraction | Resolution | 1.70 Å | Mutation | No | [1] |
| PDB Sequence |
LDPGLQPGQF
10 SADEAGAQLF20 AQSYQSSAEQ30 VLFQSVAASW40 AHDTNITAEN50 ARRQEEAALL 60 SQEFAEAWGQ70 KAKELYEPIW80 QQFTDPQLRR90 IIGAVRTLGS100 ANLPLAKRQQ 110 YNALLSQMSR120 IYSTAKVCLT135 CWSLDPDLTN145 ILASSRSYAM155 LLFAWEGWHN 165 AAGIPLKPLY175 EDFTALSNEA185 YKQDGFTDTG195 AYWRSWYNSP205 TFEDDLEHLY 215 QQLEPLYLNL225 HAFVRRALHR235 RYGDRYINLR245 GPIPAHLLGD255 MWAQTWSNIY 265 DMVVPFPDKP275 NLDVTSTMLQ285 QGWQATHMFR295 VAEEFFTSLE305 LSPMPPEFWE 315 GSMLEKPADG325 REVVCHASAW335 DFYNRKDFRI345 KQCTRVTMEQ355 LVVVHHEMGH 365 IQYFLQYKDL375 PVSLREGANP385 GFHEAIGDVL395 ALSVSTPEHL405 HKIGLLDRVT 415 NDTESDINYL425 LKMALDKIAF435 LPFGYLVDQW445 RWGVFSGRTP455 PSRYNFDWWY 465 LRTKYQGICP475 PVTRNETHFD485 AGAKFHVPNV495 TPYIRYFVSF505 VLQFQFHEAL 515 CKEAGYEGPL525 HQCDIYRSTK535 AGAKLRKVLR545 AGSSRPWQEV555 LKDMVGLDAL 565 DAQPLLKYFQ575 LVTQWLQEQN585 QQNGEVLGWP595 EYQWHPPLPD605 NYP |
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|
|
GLN259
2.241
HIS331
1.865
ALA332
2.488
SER333
2.537
ALA334
2.068
TRP335
4.283
VAL358
3.185
HIS361
2.893
GLU362
2.725
HIS365
2.979
PHE369
3.174
HIS388
3.621
|
|||||
| PDB ID: 6EN5 Crystal structure A of the Angiotensin-1 converting enzyme N-domain in complex with a diprolyl inhibitor. | ||||||
| Method | X-ray diffraction | Resolution | 1.75 Å | Mutation | No | [2] |
| PDB Sequence |
LDPGLQPGQF
10 SADEAGAQLF20 AQSYQSSAEQ30 VLFQSVAASW40 AHDTNITAEN50 ARRQEEAALL 60 SQEFAEAWGQ70 KAKELYEPIW80 QQFTDPQLRR90 IIGAVRTLGS100 ANLPLAKRQQ 110 YNALLSQMSR120 IYSTAKVCLP130 CWSLDPDLTN145 ILASSRSYAM155 LLFAWEGWHN 165 AAGIPLKPLY175 EDFTALSNEA185 YKQDGFTDTG195 AYWRSWYNSP205 TFEDDLEHLY 215 QQLEPLYLNL225 HAFVRRALHR235 RYGDRYINLR245 GPIPAHLLGD255 MWAQSWENIY 265 DMVVPFPDKP275 NLDVTSTMLQ285 QGWQATHMFR295 VAEEFFTSLE305 LSPMPPEFWE 315 GSMLEKPADG325 REVVCHASAW335 DFYNRKDFRI345 KQCTRVTMDQ355 LSTVHHEMGH 365 IQYYLQYKDL375 PVSLRRGANP385 GFHEAIGDVL395 ALSVSTPEHL405 HKIGLLDRVT 415 NDTESDINYL425 LKMALEKIAF435 LPFGYLVDQW445 RWGVFSGRTP455 PSRYNFDWWY 465 LRTKYQGICP475 PVTRNETHFD485 AGAKFHVPNV495 TPYIRYFVSF505 VLQFQFHEAL 515 CKEAGYEGPL525 HQCDIYRSTK535 AGAKLRKVLR545 AGSSRPWQEV555 LKDMVGLDAL 565 DAQPLLKYFQ575 LVTQWLQEQN585 QQNGEVLGWP595 EYQWHPPLPD605 NYPEG |
|||||
|
|
GLN259
2.411
HIS331
2.123
ALA332
2.123
SER333
2.463
ALA334
2.101
TRP335
4.356
THR358
3.045
HIS361
2.894
GLU362
2.780
HIS365
2.830
TYR369
1.897
HIS388
3.930
|
|||||
| PDB ID: 6EN6 Crystal structure B of the Angiotensin-1 converting enzyme N-domain in complex with a diprolyl inhibitor. | ||||||
| Method | X-ray diffraction | Resolution | 1.80 Å | Mutation | No | [2] |
| PDB Sequence |
LDPGLQPGQF
10 SADEAGAQLF20 AQSYQSSAEQ30 VLFQSVAASW40 AHDTNITAEN50 ARRQEEAALL 60 SQEFAEAWGQ70 KAKELYEPIW80 QQFTDPQLRR90 IIGAVRTLGS100 ANLPLAKRQQ 110 YNALLSQMSR120 IYSTAKVCLP130 CWSLDPDLTN145 ILASSRSYAM155 LLFAWEGWHN 165 AAGIPLKPLY175 EDFTALSNEA185 YKQDGFTDTG195 AYWRSWYNSP205 TFEDDLEHLY 215 QQLEPLYLNL225 HAFVRRALHR235 RYGDRYINLR245 GPIPAHLLGD255 MWAQSWENIY 265 DMVVPFPDKP275 NLDVTSTMLQ285 QGWQATHMFR295 VAEEFFTSLE305 LSPMPPEFWE 315 GSMLEKPADG325 REVVCHASAW335 DFYNRKDFRI345 KQCTRVTMDQ355 LSTVHHEMGH 365 IQYYLQYKDL375 PVSLRRGANP385 GFHEAIGDVL395 ALSVSTPEHL405 HKIGLLDRVT 415 NDTESDINYL425 LKMALEKIAF435 LPFGYLVDQW445 RWGVFSGRTP455 PSRYNFDWWY 465 LRTKYQGICP475 PVTRNETHFD485 AGAKFHVPNV495 TPYIRYFVSF505 VLQFQFHEAL 515 CKEAGYEGPL525 HQCDIYRSTK535 AGAKLRKVLR545 AGSSRPWQEV555 LKDMVGLDAL 565 DAQPLLKYFQ575 LVTQWLQEQN585 QQNGEVLGWP595 EYQWHPPLPD605 NYPEG |
|||||
|
|
GLN259
2.328
HIS331
1.736
ALA332
2.169
SER333
2.400
ALA334
2.056
TRP335
4.191
THR358
2.997
HIS361
2.850
GLU362
2.762
HIS365
2.941
TYR369
1.780
HIS388
3.859
|
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| References | Top | ||||
|---|---|---|---|---|---|
| REF 1 | ACE-domain selectivity extends beyond direct interacting residues at the active site. Biochem J. 2020 Apr 17;477(7):1241-1259. | ||||
| REF 2 | The Design and Development of a Potent and Selective Novel Diprolyl Derivative That Binds to the N-Domain of Angiotensin-I Converting Enzyme. J Med Chem. 2018 Jan 11;61(1):344-359. | ||||
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