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- PDB-2alr: ALDEHYDE REDUCTASE -

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ID or keywords:

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Basic information

Entry
Database: PDB / ID: 2alr
TitleALDEHYDE REDUCTASE
ComponentsALDEHYDE REDUCTASEAldose reductase
KeywordsOXIDOREDUCTASE / TIM-BARREL
Function / homology
Function and homology information


glucuronate reductase / glucuronolactone reductase / glucuronolactone reductase activity / glucuronate catabolic process to xylulose 5-phosphate / Formation of xylulose-5-phosphate / D-glucuronate catabolic process / alcohol dehydrogenase (NADP+) / aldehyde catabolic process / alcohol dehydrogenase (NADP+) activity / cellular aldehyde metabolic process ...glucuronate reductase / glucuronolactone reductase / glucuronolactone reductase activity / glucuronate catabolic process to xylulose 5-phosphate / Formation of xylulose-5-phosphate / D-glucuronate catabolic process / alcohol dehydrogenase (NADP+) / aldehyde catabolic process / alcohol dehydrogenase (NADP+) activity / cellular aldehyde metabolic process / cellular detoxification of aldehyde / glutathione derivative biosynthetic process / aldo-keto reductase (NADPH) activity / L-glucuronate reductase activity / D/L-glyceraldehyde reductase / Glutathione conjugation / L-ascorbic acid biosynthetic process / allyl-alcohol dehydrogenase / allyl-alcohol dehydrogenase activity / daunorubicin metabolic process / doxorubicin metabolic process / aldose reductase (NADPH) activity / glucose metabolic process / electron transfer activity / oxidoreductase activity / apical plasma membrane / extracellular space / extracellular exosome / cytosol
Similarity search - Function
Aldo/keto reductase family putative active site signature. / Aldo/keto reductase family signature 1. / NADP-dependent oxidoreductase domain / Aldo/keto reductase family signature 2. / Aldo/keto reductase, conserved site / Aldo-keto reductase / NADP-dependent oxidoreductase domain / Aldo/keto reductase family / NADP-dependent oxidoreductase domain superfamily / TIM Barrel ...Aldo/keto reductase family putative active site signature. / Aldo/keto reductase family signature 1. / NADP-dependent oxidoreductase domain / Aldo/keto reductase family signature 2. / Aldo/keto reductase, conserved site / Aldo-keto reductase / NADP-dependent oxidoreductase domain / Aldo/keto reductase family / NADP-dependent oxidoreductase domain superfamily / TIM Barrel / Alpha-Beta Barrel / Alpha Beta
Similarity search - Domain/homology
Aldo-keto reductase family 1 member A1
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / Resolution: 2.48 Å
AuthorsEl-Kabbani, O.
Citation
Journal: Acta Crystallogr.,Sect.D / Year: 1994
Title: Structures of human and porcine aldehyde reductase: an enzyme implicated in diabetic complications.
Authors: El-Kabbani, O. / Green, N.C. / Lin, G. / Carson, M. / Narayana, S.V. / Moore, K.M. / Flynn, T.G. / DeLucas, L.J.
#1: Journal: Acta Crystallogr.,Sect.D / Year: 1993
Title: Crystallization and Preliminary Structure Determination of Porcine Aldehyde Reductase from Two Crystal Forms
Authors: El-Kabbani, O. / Lin, G. / Narayana, S.V.L. / Moore, K.M. / Green, N.C. / Flynn, T.G. / Delucas, L.J.
History
DepositionSep 6, 1994Processing site: BNL
SupersessionJun 20, 1996ID: 1ALR
Revision 1.0Jun 20, 1996Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 14, 2024Group: Data collection / Database references / Other
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.process_site

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: ALDEHYDE REDUCTASE


Theoretical massNumber of molelcules
Total (without water)36,4871
Polymers36,4871
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)82.600, 60.000, 66.200
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

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Components

#1: Protein ALDEHYDE REDUCTASE / Aldose reductase / ALR1


Mass: 36486.770 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Organ: KIDNEY / Tissue: MEDULLA, CORTEX / References: UniProt: P14550, alcohol dehydrogenase (NADP+)

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 2.25 Å3/Da / Density % sol: 43 %
Crystal growpH: 6.2 / Details: pH 6.2
Crystal
*PLUS
Crystal grow
*PLUS
Temperature: 293 K / pH: 6.4 / Method: vapor diffusion, hanging drop
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-ID
120 %ammonium salfate1drop
210 mMPIPES1drop
32 mM2-mercaptoethanol1drop
420 mMbeta-octylglucoside1drop
535 %ammonium sulfate1reservoir
650 mMPIPES1reservoir
72 mM2-mercaptoethanol1reservoir
820 mMbeta-octylglucoside1reservoir

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Data collection

DiffractionMean temperature: 293 K
Diffraction sourceWavelength: 1.5418
DetectorType: SIEMENS / Detector: AREA DETECTOR / Date: Apr 14, 1992 / Details: COLLIMATOR
RadiationMonochromator: GRAPHITE(002) / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.5418 Å / Relative weight: 1
ReflectionNum. obs: 10591 / % possible obs: 92 % / Observed criterion σ(I): 0 / Redundancy: 0.98 % / Rmerge(I) obs: 0.083

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Processing

Software
NameClassification
X-PLORmodel building
TNTrefinement
X-PLORrefinement
XENGENdata reduction
X-PLORphasing
RefinementResolution: 2.48→6 Å / σ(F): 4 /
RfactorNum. reflection
Rwork0.19 -
obs-9538
Refinement stepCycle: LAST / Resolution: 2.48→6 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2472 0 0 0 2472
Refine LS restraints
Refine-IDTypeDev idealWeight
X-RAY DIFFRACTIONt_bond_d0.0060.02
X-RAY DIFFRACTIONt_angle_deg2.13
X-RAY DIFFRACTIONt_dihedral_angle_d17.815
X-RAY DIFFRACTIONt_incorr_chiral_ct0
X-RAY DIFFRACTIONt_pseud_angle
X-RAY DIFFRACTIONt_trig_c_planes0.0040.02
X-RAY DIFFRACTIONt_gen_planes0.0080.02
X-RAY DIFFRACTIONt_it
X-RAY DIFFRACTIONt_nbd
Software
*PLUS
Name: TNT / Classification: refinement
Refinement
*PLUS
Rfactor obs: 0.19
Solvent computation
*PLUS
Displacement parameters
*PLUS

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