Target Binding Site Detail
| Target General Information | Top | ||||
|---|---|---|---|---|---|
| Target ID | T83011 | Target Info | |||
| Target Name | Monoamine oxidase type B (MAO-B) | ||||
| Synonyms | MAO-B; Amine oxidase [flavin-containing] B | ||||
| Target Type | Successful Target | ||||
| Gene Name | MAOB | ||||
| Biochemical Class | CH-NH(2) donor oxidoreductase | ||||
| UniProt ID | |||||
| Ligand General Information | Top | ||||
|---|---|---|---|---|---|
| Ligand Name | N-Propargyl-1(S)-Aminoindan | Ligand Info | |||
| Canonical SMILES | C#CCNC1CCC2=CC=CC=C12 | ||||
| InChI | 1S/C12H13N/c1-2-9-13-12-8-7-10-5-3-4-6-11(10)12/h1,3-6,12-13H,7-9H2/t12-/m0/s1 | ||||
| InChIKey | RUOKEQAAGRXIBM-LBPRGKRZSA-N | ||||
| PubChem Compound ID | 5289310 | ||||
| Drug Binding Sites of Target | Top | |||||
|---|---|---|---|---|---|---|
| PDB ID: 2C75 Functional Role of the Aromatic Cage in Human Monoamine Oxidase B: Structures and Catalytic Properties of Tyr435 Mutant Proteins | ||||||
| Method | X-ray diffraction | Resolution | 1.70 Å | Mutation | Yes | [1] |
| PDB Sequence |
NKCDVVVVGG
12 GISGMAAAKL22 LHDSGLNVVV32 LEARDRVGGR42 TYTLRNQKVK52 YVDLGGSYVG 62 PTQNRILRLA72 KELGLETYKV82 NEVERLIHHV92 KGKSYPFRGP102 FPPVWNPITY 112 LDHNNFWRTM122 DDMGREIPSD132 APWKAPLAEE142 WDNMTMKELL152 DKLCWTESAK 162 QLATLFVNLC172 VTAETHEVSA182 LWFLWYVKQC192 GGTTRIISTT202 NGGQERKFVG 212 GSGQVSERIM222 DLLGDRVKLE232 RPVIYIDQTR242 ENVLVETLNH252 EMYEAKYVIS 262 AIPPTLGMKI272 HFNPPLPMMR282 NQMITRVPLG292 SVIKCIVYYK302 EPFWRKKDYC 312 GTMIIDGEEA322 PVAYTLDDTK332 PEGNYAAIMG342 FILAHKARKL352 ARLTKEERLK 362 KLCELYAKVL372 GSLEALEPVH382 YEEKNWCEEQ392 YSGGCYTTYF402 PPGILTQYGR 412 VLRQPVDRIY422 FAGTETATHW432 SGLMEGAVEA442 GERAAREILH452 AMGKIPEDEI 462 WQSEPESVDV472 PAQPITTTFL482 ERHLPSVPGL492 LRLIGLTTI
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| PDB ID: 2C76 Functional Role of the Aromatic Cage in Human Monoamine Oxidase B: Structures and Catalytic Properties of Tyr435 Mutant Proteins | ||||||
| Method | X-ray diffraction | Resolution | 1.70 Å | Mutation | Yes | [1] |
| PDB Sequence |
NKCDVVVVGG
12 GISGMAAAKL22 LHDSGLNVVV32 LEARDRVGGR42 TYTLRNQKVK52 YVDLGGSYVG 62 PTQNRILRLA72 KELGLETYKV82 NEVERLIHHV92 KGKSYPFRGP102 FPPVWNPITY 112 LDHNNFWRTM122 DDMGREIPSD132 APWKAPLAEE142 WDNMTMKELL152 DKLCWTESAK 162 QLATLFVNLC172 VTAETHEVSA182 LWFLWYVKQC192 GGTTRIISTT202 NGGQERKFVG 212 GSGQVSERIM222 DLLGDRVKLE232 RPVIYIDQTR242 ENVLVETLNH252 EMYEAKYVIS 262 AIPPTLGMKI272 HFNPPLPMMR282 NQMITRVPLG292 SVIKCIVYYK302 EPFWRKKDYC 312 GTMIIDGEEA322 PVAYTLDDTK332 PEGNYAAIMG342 FILAHKARKL352 ARLTKEERLK 362 KLCELYAKVL372 GSLEALEPVH382 YEEKNWCEEQ392 YSGGCYTTYF402 PPGILTQYGR 412 VLRQPVDRIY422 FAGTETATHW432 SGWMEGAVEA442 GERAAREILH452 AMGKIPEDEI 462 WQSEPESVDV472 PAQPITTTFL482 ERHLPSVPGL492 LRLIGLTTI
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| PDB ID: 2C72 Functional Role of the Aromatic Cage in Human Monoamine Oxidase B: Structures and Catalytic Properties of Tyr435 Mutant Proteins | ||||||
| Method | X-ray diffraction | Resolution | 2.00 Å | Mutation | Yes | [1] |
| PDB Sequence |
NKCDVVVVGG
12 GISGMAAAKL22 LHDSGLNVVV32 LEARDRVGGR42 TYTLRNQKVK52 YVDLGGSYVG 62 PTQNRILRLA72 KELGLETYKV82 NEVERLIHHV92 KGKSYPFRGP102 FPPVWNPITY 112 LDHNNFWRTM122 DDMGREIPSD132 APWKAPLAEE142 WDNMTMKELL152 DKLCWTESAK 162 QLATLFVNLC172 VTAETHEVSA182 LWFLWYVKQC192 GGTTRIISTT202 NGGQERKFVG 212 GSGQVSERIM222 DLLGDRVKLE232 RPVIYIDQTR242 ENVLVETLNH252 EMYEAKYVIS 262 AIPPTLGMKI272 HFNPPLPMMR282 NQMITRVPLG292 SVIKCIVYYK302 EPFWRKKDYC 312 GTMIIDGEEA322 PVAYTLDDTK332 PEGNYAAIMG342 FILAHKARKL352 ARLTKEERLK 362 KLCELYAKVL372 GSLEALEPVH382 YEEKNWCEEQ392 YSGGCYTTYF402 PPGILTQYGR 412 VLRQPVDRIY422 FAGTETATHW432 SGHMEGAVEA442 GERAAREILH452 AMGKIPEDEI 462 WQSEPESVDV472 PAQPITTTFL482 ERHLPSVPGL492 LRLIGLTTI
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| PDB ID: 1S2Y Crystal structure of MAOB in complex with N-propargyl-1(S)-aminoindan | ||||||
| Method | X-ray diffraction | Resolution | 2.12 Å | Mutation | No | [2] |
| PDB Sequence |
NKCDVVVVGG
12 GISGMAAAKL22 LHDSGLNVVV32 LEARDRVGGR42 TYTLRNQKVK52 YVDLGGSYVG 62 PTQNRILRLA72 KELGLETYKV82 NEVERLIHHV92 KGKSYPFRGP102 FPPVWNPITY 112 LDHNNFWRTM122 DDMGREIPSD132 APWKAPLAEE142 WDNMTMKELL152 DKLCWTESAK 162 QLATLFVNLC172 VTAETHEVSA182 LWFLWYVKQC192 GGTTRIISTT202 NGGQERKFVG 212 GSGQVSERIM222 DLLGDRVKLE232 RPVIYIDQTR242 ENVLVETLNH252 EMYEAKYVIS 262 AIPPTLGMKI272 HFNPPLPMMR282 NQMITRVPLG292 SVIKCIVYYK302 EPFWRKKDYC 312 GTMIIDGEEA322 PVAYTLDDTK332 PEGNYAAIMG342 FILAHKARKL352 ARLTKEERLK 362 KLCELYAKVL372 GSLEALEPVH382 YEEKNWCEEQ392 YSGGCYTTYF402 PPGILTQYGR 412 VLRQPVDRIY422 FAGTETATHW432 SGYMEGAVEA442 GERAAREILH452 AMGKIPEDEI 462 WQSEPESVDV472 PAQPITTTFL482 ERHLPSVPGL492 LRLIGLTTI
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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 .RSA or .RSA2 or .RSA3 or :3RSA;style chemicals stick;color identity;select .A:60 or .A:171 or .A:172 or .A:198 or .A:199 or .A:206 or .A:326 or .A:328 or .A:343 or .A:398 or .A:435; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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| PDB ID: 2C73 Functional Role of the Aromatic Cage in Human Monoamine Oxidase B: Structures and Catalytic Properties of Tyr435 Mutant Proteins | ||||||
| Method | X-ray diffraction | Resolution | 2.20 Å | Mutation | Yes | [1] |
| PDB Sequence |
NKCDVVVVGG
12 GISGMAAAKL22 LHDSGLNVVV32 LEARDRVGGR42 TYTLRNQKVK52 YVDLGGSYVG 62 PTQNRILRLA72 KELGLETYKV82 NEVERLIHHV92 KGKSYPFRGP102 FPPVWNPITY 112 LDHNNFWRTM122 DDMGREIPSD132 APWKAPLAEE142 WDNMTMKELL152 DKLCWTESAK 162 QLATLFVNLC172 VTAETHEVSA182 LWFLWYVKQC192 GGTTRIISTT202 NGGQERKFVG 212 GSGQVSERIM222 DLLGDRVKLE232 RPVIYIDQTR242 ENVLVETLNH252 EMYEAKYVIS 262 AIPPTLGMKI272 HFNPPLPMMR282 NQMITRVPLG292 SVIKCIVYYK302 EPFWRKKDYC 312 GTMIIDGEEA322 PVAYTLDDTK332 PEGNYAAIMG342 FILAHKARKL352 ARLTKEERLK 362 KLCELYAKVL372 GSLEALEPVH382 YEEKNWCEEQ392 YSGGCYTTYF402 PPGILTQYGR 412 VLRQPVDRIY422 FAGTETATHW432 SGFMEGAVEA442 GERAAREILH452 AMGKIPEDEI 462 WQSEPESVDV472 PAQPITTTFL482 ERHLPSVPGL492 LRLIGLTTI
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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 .RSA or .RSA2 or .RSA3 or :3RSA;style chemicals stick;color identity;select .A:58 or .A:59 or .A:60 or .A:168 or .A:171 or .A:172 or .A:198 or .A:199 or .A:206 or .A:326 or .A:343 or .A:398 or .A:435; 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 | Functional role of the "aromatic cage" in human monoamine oxidase B: structures and catalytic properties of Tyr435 mutant proteins. Biochemistry. 2006 Apr 18;45(15):4775-84. | ||||
| REF 2 | Crystal structures of monoamine oxidase B in complex with four inhibitors of the N-propargylaminoindan class. J Med Chem. 2004 Mar 25;47(7):1767-74. | ||||
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