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 | (2-{[(4-Bromo-2-Fluorobenzyl)amino]carbonyl}-5-Chlorophenoxy)acetic Acid | Ligand Info | |||
| Canonical SMILES | C1=CC(=C(C=C1Cl)OCC(=O)O)C(=O)NCC2=C(C=C(C=C2)Br)F | ||||
| InChI | 1S/C16H12BrClFNO4/c17-10-2-1-9(13(19)5-10)7-20-16(23)12-4-3-11(18)6-14(12)24-8-15(21)22/h1-6H,7-8H2,(H,20,23)(H,21,22) | ||||
| InChIKey | ZLIGBZRXAQNUFO-UHFFFAOYSA-N | ||||
| PubChem Compound ID | 16058629 | ||||
| Drug Binding Sites of Target | Top | |||||
|---|---|---|---|---|---|---|
| PDB ID: 3M4H Human Aldose Reductase mutant T113V complexed with IDD388 | ||||||
| Method | X-ray diffraction | Resolution | 0.94 Å | Mutation | Yes | [1] |
| 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
|
|||||
|
|
||||||
| PDB ID: 3LEP Human Aldose Reductase mutant T113C in complex with IDD388 | ||||||
| Method | X-ray diffraction | Resolution | 0.99 Å | Mutation | Yes | [1] |
| PDB Sequence |
MASRILLNNG
9 AKMPILGLGT19 WKSPPGQVTE29 AVKVAIDVGY39 RHIDCAHVYQ49 NENEVGVAIQ 59 EKLREQVVKR69 EELFIVSKLW79 CTYHEKGLVK89 GACQKTLSDL99 KLDYLDLYLI 109 HWPCGFKPGK119 EFFPLDESGN129 VVPSDTNILD139 TWAAMEELVD149 EGLVKAIGIS 159 NFNHLQVEMI169 LNKPGLKYKP179 AVNQIECHPY189 LTQEKLIQYC199 QSKGIVVTAY 209 SPLGSPDRPW219 AKPEDPSLLE229 DPRIKAIAAK239 HNKTTAQVLI249 RFPMQRNLVV 259 IPKSVTPERI269 AENFKVFDFE279 LSSQDMTTLL289 SYNRNWRVCA299 LLSCTSHKDY 309 PFHE
|
|||||
|
|
||||||
| PDB ID: 3LZ3 Human aldose reductase mutant T113S complexed with IDD388 | ||||||
| Method | X-ray diffraction | Resolution | 1.03 Å | Mutation | Yes | [1] |
| PDB Sequence |
MASRILLNNG
9 AKMPILGLGT19 WKSPPGQVTE29 AVKVAIDVGY39 RHIDCAHVYQ49 NENEVGVAIQ 59 EKLREQVVKR69 EELFIVSKLW79 CTYHEKGLVK89 GACQKTLSDL99 KLDYLDLYLI 109 HWPSGFKPGK119 EFFPLDESGN129 VVPSDTNILD139 TWAAMEELVD149 EGLVKAIGIS 159 NFNHLQVEMI169 LNKPGLKYKP179 AVNQIECHPY189 LTQEKLIQYC199 QSKGIVVTAY 209 SPLGSPDRPW219 AKPEDPSLLE229 DPRIKAIAAK239 HNKTTAQVLI249 RFPMQRNLVV 259 IPKSVTPERI269 AENFKVFDFE279 LSSQDMTTLL289 SYNRNWRVCA299 LLSCTSHKDY 309 PFH
|
|||||
|
|
||||||
| PDB ID: 3LQG Human aldose reductase mutant T113A complexed with IDD388 | ||||||
| Method | X-ray diffraction | Resolution | 1.35 Å | Mutation | Yes | [1] |
| PDB Sequence |
SRILLNNGAK
11 MPILGLGTWK21 SPPGQVTEAV31 KVAIDVGYRH41 IDCAHVYQNE51 NEVGVAIQEK 61 LREQVVKREE71 LFIVSKLWCT81 YHEKGLVKGA91 CQKTLSDLKL101 DYLDLYLIHW 111 PAGFKPGKEF121 FPLDESGNVV131 PSDTNILDTW141 AAMEELVDEG151 LVKAIGISNF 161 NHLQVEMILN171 KPGLKYKPAV181 NQIECHPYLT191 QEKLIQYCQS201 KGIVVTAYSP 211 LGSPDRPWAK221 PEDPSLLEDP231 RIKAIAAKHN241 KTTAQVLIRF251 PMQRNLVVIP 261 KSVTPERIAE271 NFKVFDFELS281 SQDMTTLLSY291 NRNWRVCALL301 SCTSHKDYPF 311 H
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .388 or .3882 or .3883 or :3388;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:311; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
||||||
| PDB ID: 2IKI Human aldose reductase complexed with halogenated IDD-type inhibitor | ||||||
| Method | X-ray diffraction | Resolution | 1.47 Å | Mutation | No | [2] |
| 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 F
|
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .388 or .3882 or .3883 or :3388;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:311; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
||||||
| References | Top | ||||
|---|---|---|---|---|---|
| REF 1 | Tracing the detail: how mutations affect binding modes and thermodynamic signatures of closely related aldose reductase inhibitors. J Mol Biol. 2011 Mar 11;406(5):700-12. | ||||
| REF 2 | 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. | ||||
If You Find Any Error in Data or Bug in Web Service, Please Kindly Report It to Dr. Zhou and Dr. Zhang.