Target Binding Site Detail
| Target General Information | Top | ||||
|---|---|---|---|---|---|
| Target ID | T26623 | Target Info | |||
| Target Name | Aldose reductase (AKR1B1) | ||||
| Synonyms | Aldehyde reductase; AKR1B1 | ||||
| Target Type | Successful Target | ||||
| Gene Name | AKR1B1 | ||||
| Biochemical Class | Short-chain dehydrogenases reductase | ||||
| UniProt ID | |||||
| Ligand General Information | Top | ||||
|---|---|---|---|---|---|
| Ligand Name | (5-Chloro-2-{[(3-Nitrobenzyl)amino]carbonyl}phenoxy)acetic Acid | Ligand Info | |||
| Canonical SMILES | C1=CC(=CC(=C1)[N+](=O)[O-])CNC(=O)C2=C(C=C(C=C2)Cl)OCC(=O)O | ||||
| InChI | 1S/C16H13ClN2O6/c17-11-4-5-13(14(7-11)25-9-15(20)21)16(22)18-8-10-2-1-3-12(6-10)19(23)24/h1-7H,8-9H2,(H,18,22)(H,20,21) | ||||
| InChIKey | VABIMMIJVWNHFI-UHFFFAOYSA-N | ||||
| PubChem Compound ID | 16058630 | ||||
| Drug Binding Sites of Target | Top | |||||
|---|---|---|---|---|---|---|
| PDB ID: 2PZN The crystallographic structure of Aldose Reductase IDD393 complex confirms Leu300 as a specificity determinant | ||||||
| Method | X-ray diffraction | Resolution | 1.00 Å | Mutation | No | [1] |
| PDB Sequence |
MASRILLNNG
9 AKMPILGLGT19 WKSPPGQVTE29 AVKVAIDVGY39 RHIDCAHVYQ49 NENEVGVAIQ 59 EKLREQVVKR69 EELFIVSKLW79 CTYHEKGLVK89 GACQKTLSDL99 KLDYLDLYLI 109 HWPTGFKPGK119 EFFPLDESGN129 VVPSDTNILD139 TWAAMEELVD149 EGLVKAIGIS 159 NFNHLQVEMI169 LNKPGLKYKP179 AVNQIECHPY189 LTQEKLIQYC199 QSKGIVVTAY 209 SPLGSPDRPW219 AKPEDPSLLE229 DPRIKAIAAK239 HNKTTAQVLI249 RFPMQRNLVV 259 IPKSVTPERI269 AENFKVFDFE279 LSSQDMTTLL289 SYNRNWRVCA299 LLSCTSHKDY 309 PFHEEF
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| PDB ID: 3MC5 Human Aldose Reductase mutant T113V in complex with IDD393 crystallized in spacegroup P1 | ||||||
| Method | X-ray diffraction | Resolution | 1.14 Å | Mutation | Yes | [2] |
| PDB Sequence |
MASRILLNNG
9 AKMPILGLGT19 WKSPPGQVTE29 AVKVAIDVGY39 RHIDCAHVYQ49 NENEVGVAIQ 59 EKLREQVVKR69 EELFIVSKLW79 CTYHEKGLVK89 GACQKTLSDL99 KLDYLDLYLI 109 HWPVGFKPGK119 EFFPLDESGN129 VVPSDTNILD139 TWAAMEELVD149 EGLVKAIGIS 159 NFNHLQVEMI169 LNKPGLKYKP179 AVNQIECHPY189 LTQEKLIQYC199 QSKGIVVTAY 209 SPLGSPDRPW219 AKPEDPSLLE229 DPRIKAIAAK239 HNKTTAQVLI249 RFPMQRNLVV 259 IPKSVTPERI269 AENFKVFDFE279 LSSQDMTTLL289 SYNRNWRVCA299 LLSCTSHKDY 309 PFHEEF
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| PDB ID: 3M64 Human aldose reductase mutant T113V complexed with IDD393 | ||||||
| Method | X-ray diffraction | Resolution | 1.30 Å | Mutation | Yes | [2] |
| PDB Sequence |
MASRILLNNG
9 AKMPILGLGT19 WKSPPGQVTE29 AVKVAIDVGY39 RHIDCAHVYQ49 NENEVGVAIQ 59 EKLREQVVKR69 EELFIVSKLW79 CTYHEKGLVK89 GACQKTLSDL99 KLDYLDLYLI 109 HWPVGFKPGK119 EFFPLDESGN129 VVPSDTNILD139 TWAAMEELVD149 EGLVKAIGIS 159 NFNHLQVEMI169 LNKPGLKYKP179 AVNQIECHPY189 LTQEKLIQYC199 QSKGIVVTAY 209 SPLGSPDRPW219 AKPEDPSLLE229 DPRIKAIAAK239 HNKTTAQVLI249 RFPMQRNLVV 259 IPKSVTPERI269 AENFKVFDFE279 LSSQDMTTLL289 SYNRNWRVCA299 LLSCTSHKDY 309 PFHEEF
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| PDB ID: 2IKJ Human aldose reductase complexed with nitro-substituted IDD-type inhibitor | ||||||
| Method | X-ray diffraction | Resolution | 1.55 Å | Mutation | No | [3] |
| PDB Sequence |
ASRILLNNGA
10 KMPILGLGTW20 KSPPGQVTEA30 VKVAIDVGYR40 HIDCAHVYQN50 ENEVGVAIQE 60 KLREQVVKRE70 ELFIVSKLWC80 TYHEKGLVKG90 ACQKTLSDLK100 LDYLDLYLIH 110 WPTGFKPGKE120 FFPLDESGNV130 VPSDTNILDT140 WAAMEELVDE150 GLVKAIGISN 160 FNHLQVEMIL170 NKPGLKYKPA180 VNQIECHPYL190 TQEKLIQYCQ200 SKGIVVTAYS 210 PLGSPDRPWA220 KPEDPSLLED230 PRIKAIAAKH240 NKTTAQVLIR250 FPMQRNLVVI 260 PKSVTPERIA270 ENFKVFDFEL280 SSQDMTTLLS290 YNRNWRVCAL300 LSCTSHKDYP 310 FHEEF
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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 .393 or .3932 or .3933 or :3393;style chemicals stick;color identity;select .A:20 or .A:47 or .A:48 or .A:79 or .A:80 or .A:110 or .A:111 or .A:113 or .A:115 or .A:122 or .A:219 or .A:298 or .A:299 or .A:300 or .A:303 or .A:309 or .A:310 or .A:311; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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| PDB ID: 2PDU Human aldose reductase mutant C303D complexed with IDD393. | ||||||
| Method | X-ray diffraction | Resolution | 1.55 Å | Mutation | Yes | [4] |
| PDB Sequence |
ASRILLNNGA
10 KMPILGLGTW20 KSPPGQVTEA30 VKVAIDVGYR40 HIDCAHVYQN50 ENEVGVAIQE 60 KLREQVVKRE70 ELFIVSKLWC80 TYHEKGLVKG90 ACQKTLSDLK100 LDYLDLYLIH 110 WPTGFKPGKE120 FFPLDESGNV130 VPSDTNILDT140 WAAMEELVDE150 GLVKAIGISN 160 FNHLQVEMIL170 NKPGLKYKPA180 VNQIECHPYL190 TQEKLIQYCQ200 SKGIVVTAYS 210 PLGSPDRPWA220 KPEDPSLLED230 PRIKAIAAKH240 NKTTAQVLIR250 FPMQRNLVVI 260 PKSVTPERIA270 ENFKVFDFEL280 SSQDMTTLLS290 YNRNWRVCAL300 LSDTSHKDYP 310 FHEEF
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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 .393 or .3932 or .3933 or :3393;style chemicals stick;color identity;select .A:20 or .A:47 or .A:48 or .A:79 or .A:80 or .A:110 or .A:111 or .A:113 or .A:115 or .A:122 or .A:219 or .A:298 or .A:299 or .A:300 or .A:303 or .A:309 or .A:310 or .A:311; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
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| PDB ID: 2PDJ Human aldose reductase mutant L300A complexed with IDD393. | ||||||
| Method | X-ray diffraction | Resolution | 1.57 Å | Mutation | Yes | [4] |
| PDB Sequence |
ASRILLNNGA
10 KMPILGLGTW20 KSPPGQVTEA30 VKVAIDVGYR40 HIDCAHVYQN50 ENEVGVAIQE 60 KLREQVVKRE70 ELFIVSKLWC80 TYHEKGLVKG90 ACQKTLSDLK100 LDYLDLYLIH 110 WPTGFKPGKE120 FFPLDESGNV130 VPSDTNILDT140 WAAMEELVDE150 GLVKAIGISN 160 FNHLQVEMIL170 NKPGLKYKPA180 VNQIECHPYL190 TQEKLIQYCQ200 SKGIVVTAYS 210 PLGSPDRPWA220 KPEDPSLLED230 PRIKAIAAKH240 NKTTAQVLIR250 FPMQRNLVVI 260 PKSVTPERIA270 ENFKVFDFEL280 SSQDMTTLLS290 YNRNWRVCAA300 LSCTSHKDYP 310 FHEEF
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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 .393 or .3932 or .3933 or :3393;style chemicals stick;color identity;select .A:20 or .A:47 or .A:48 or .A:79 or .A:80 or .A:110 or .A:111 or .A:113 or .A:115 or .A:122 or .A:219 or .A:298 or .A:299 or .A:300 or .A:303 or .A:309 or .A:310 or .A:311; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
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| PDB ID: 2PDC Human aldose reductase mutant F121P complexed with IDD393. | ||||||
| Method | X-ray diffraction | Resolution | 1.65 Å | Mutation | Yes | [4] |
| PDB Sequence |
ASRILLNNGA
10 KMPILGLGTW20 KSPPGQVTEA30 VKVAIDVGYR40 HIDCAHVYQN50 ENEVGVAIQE 60 KLREQVVKRE70 ELFIVSKLWC80 TYHEKGLVKG90 ACQKTLSDLK100 LDYLDLYLIH 110 WPTGFKPGKE120 PFPLDESGNV130 VPSDTNILDT140 WAAMEELVDE150 GLVKAIGISN 160 FNHLQVEMIL170 NKPGLKYKPA180 VNQIECHPYL190 TQEKLIQYCQ200 SKGIVVTAYS 210 PLGSPDRPWA220 KPEDPSLLED230 PRIKAIAAKH240 NKTTAQVLIR250 FPMQRNLVVI 260 PKSVTPERIA270 ENFKVFDFEL280 SSQDMTTLLS290 YNRNWRVCAL300 LSCTSHKDYP 310 FHEEF
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .393 or .3932 or .3933 or :3393;style chemicals stick;color identity;select .A:20 or .A:47 or .A:48 or .A:79 or .A:80 or .A:110 or .A:111 or .A:113 or .A:115 or .A:122 or .A:219 or .A:298 or .A:299 or .A:300 or .A:303 or .A:309 or .A:310 or .A:311; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
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| PDB ID: 2PDP Human aldose reductase mutant S302R complexed with IDD 393. | ||||||
| Method | X-ray diffraction | Resolution | 1.65 Å | Mutation | Yes | [4] |
| PDB Sequence |
ASRILLNNGA
10 KMPILGLGTW20 KSPPGQVTEA30 VKVAIDVGYR40 HIDCAHVYQN50 ENEVGVAIQE 60 KLREQVVKRE70 ELFIVSKLWC80 TYHEKGLVKG90 ACQKTLSDLK100 LDYLDLYLIH 110 WPTGFKPGKE120 FFPLDESGNV130 VPSDTNILDT140 WAAMEELVDE150 GLVKAIGISN 160 FNHLQVEMIL170 NKPGLKYKPA180 VNQIECHPYL190 TQEKLIQYCQ200 SKGIVVTAYS 210 PLGSPDRPWA220 KPEDPSLLED230 PRIKAIAAKH240 NKTTAQVLIR250 FPMQRNLVVI 260 PKSVTPERIA270 ENFKVFDFEL280 SSQDMTTLLS290 YNRNWRVCAL300 LRCTSHKDYP 310 FHEEF
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .393 or .3932 or .3933 or :3393;style chemicals stick;color identity;select .A:20 or .A:47 or .A:48 or .A:79 or .A:80 or .A:110 or .A:111 or .A:113 or .A:115 or .A:122 or .A:219 or .A:298 or .A:299 or .A:300 or .A:303 or .A:309 or .A:310 or .A:311; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
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| References | Top | ||||
|---|---|---|---|---|---|
| REF 1 | The Crystallographic Structure of Alr2-Idd393 Complex Confirms Leu300 as a Specificity Determinant | ||||
| REF 2 | Ligand-induced fit affects binding modes and provokes changes in crystal packing of aldose reductase. Biochim Biophys Acta. 2011 Sep;1810(9):879-87. | ||||
| REF 3 | Structural and thermodynamic study on aldose reductase: nitro-substituted inhibitors with strong enthalpic binding contribution. J Mol Biol. 2007 May 4;368(3):618-38. | ||||
| REF 4 | Merging the binding sites of aldose and aldehyde reductase for detection of inhibitor selectivity-determining features. J Mol Biol. 2008 Jun 20;379(5):991-1016. | ||||
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