Download MendeleyAldose Reductase: How expensive is the opening of the specificity pocket? IDD ligands under investigation
Rechlin, C., Scheer, F., Toth, P., Heine, A., Diederich, W., Klebe, G.To be published.
4QBX
Human Aldose Reductase complexed with a ligand with an IDD structure ({5-fluoro-2-[(3-nitrobenzyl)carbamoyl]phenoxy}acetic acid) at 0.98 A
- PDB DOI: https://doi.org/10.2210/pdb4QBX/pdb
- Classification: oxidoreductase/oxidoreductase inhibitor
- Organism(s): Homo sapiens
- Expression System: Escherichia coli BL21
- Mutation(s): No
- Deposited: 2014-05-09 Released: 2015-07-22
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 0.98 ?
- R-Value Free: 0.151
- R-Value Work: 0.135
- R-Value Observed: 0.136
Starting Model: experimental
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This is version 1.1 of the entry. See complete history.
Literature
To be published.
Macromolecules
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 1 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| Aldose reductase | 316 | Homo sapiens | Mutation(s): 0 Gene Names: AKR1B1, ALDR1 EC: 1.1.1.21 (PDB Primary Data), 1.1.1.372 (UniProt), 1.1.1.300 (UniProt), 1.1.1.54 (UniProt) |  | |
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for P15121 (Homo sapiens) Explore P15121 Go to UniProtKB: P15121 | |||||
PHAROS: P15121 GTEx: ENSG00000085662 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | P15121 | ||||
Sequence AnnotationsExpand | |||||
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Small Molecules
| Ligands 3 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| NAP Query on NAP | B [auth A] | NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE C21 H28 N7 O17 P3 XJLXINKUBYWONI-NNYOXOHSSA-N |  | ||
| 30L Query on 30L | C [auth A] | {5-fluoro-2-[(3-nitrobenzyl)carbamoyl]phenoxy}acetic acid C16 H13 F N2 O6 HOFFXZBMYHZMTN-UHFFFAOYSA-N |  | ||
| CIT Query on CIT | D [auth A] | CITRIC ACID C6 H8 O7 KRKNYBCHXYNGOX-UHFFFAOYSA-N |  | ||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 0.98 ?
- R-Value Free: 0.151
- R-Value Work: 0.135
- R-Value Observed: 0.136
- Space Group: P 1 21 1
Unit Cell:
| Length ( ? ) | Angle ( ? ) |
|---|---|
| a = 49.383 | ¦Á = 90 |
| b = 66.856 | ¦Â = 92.27 |
| c = 47.405 | ¦Ă = 90 |
| Software Name | Purpose |
|---|---|
| MAR345dtb | data collection |
| PHASER | phasing |
| PHENIX | refinement |
| HKL-2000 | data reduction |
| HKL-2000 | data scaling |
Entry History
Deposition Data
- Released Date: 2015-07-22 Deposition Author(s): Rechlin, C., Heine, A., Klebe, G.
Revision History (Full details and data files)
- Version 1.0: 2015-07-22
Type: Initial release - Version 1.1: 2023-09-20
Changes: Data collection, Database references, Derived calculations, Refinement description
