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- PDB-2alr: ALDEHYDE REDUCTASE -

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Basic information

Entry
Database: PDB / ID: 2alr
TitleALDEHYDE REDUCTASE
ComponentsALDEHYDE REDUCTASEAldose reductase
KeywordsOXIDOREDUCTASE / TIM-BARREL
Function / homologyAldo/keto reductase family / Aldo/keto reductase family signature 1. / NADP-dependent oxidoreductase domain superfamily / NADP-dependent oxidoreductase domain / Aldo/keto reductase / Aldo/keto reductase, conserved site / Aldo/keto reductase family putative active site signature. / Formation of xylulose-5-phosphate / Glutathione conjugation / Aldo/keto reductase family signature 2. ...Aldo/keto reductase family / Aldo/keto reductase family signature 1. / NADP-dependent oxidoreductase domain superfamily / NADP-dependent oxidoreductase domain / Aldo/keto reductase / Aldo/keto reductase, conserved site / Aldo/keto reductase family putative active site signature. / Formation of xylulose-5-phosphate / Glutathione conjugation / Aldo/keto reductase family signature 2. / glucuronolactone reductase activity / L-glucuronate reductase activity / glucuronate reductase / glucuronolactone reductase / D/L-glyceraldehyde reductase / glucuronate catabolic process to xylulose 5-phosphate / D-glucuronate catabolic process / alcohol dehydrogenase (NADP+) / L-ascorbic acid biosynthetic process / aldehyde catabolic process / allyl-alcohol dehydrogenase / cellular detoxification of aldehyde / cellular aldehyde metabolic process / aldo-keto reductase (NADP) activity / glutathione derivative biosynthetic process / alditol:NADP+ 1-oxidoreductase activity / alcohol dehydrogenase (NADP+) activity / glucose metabolic process / apical plasma membrane / electron transfer activity / synapse / oxidoreductase activity / extracellular space / extracellular exosome / cytosol / Aldo-keto reductase family 1 member A1
Function and homology information
Specimen sourceHomo sapiens (human)
MethodX-RAY DIFFRACTION / 2.48 Å resolution
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.
Validation Report
SummaryFull reportAbout validation report
DateDeposition: Sep 6, 1994 / Release: Jun 20, 1996
RevisionDateData content typeGroupProviderType
1.0Jun 20, 1996Structure modelrepositoryInitial release
1.1Mar 24, 2008Structure modelVersion format compliance
1.2Jul 13, 2011Structure modelVersion format compliance

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: ALDEHYDE REDUCTASE


Theoretical massNumber of molelcules
Total (without water)36,4871
Polyers36,4871
Non-polymers00
Water0
1


TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
γ
α
β
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-MP 21 21 21

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Components

#1: Protein/peptide ALDEHYDE REDUCTASE / Aldose reductase / ALR1


Mass: 36486.770 Da / Num. of mol.: 1 / Source: (natural) Homo sapiens (human) / Genus: Homo / 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 / Density percent sol: 43 %
Crystal growpH: 6.2 / Details: pH 6.2
Crystal grow
*PLUS
Temp: 293 K / pH: 6.4 / Method: vapor diffusion, hanging drop
components of the solutions
*PLUS
IDConcCommon 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 kelvins
SourceWavelength: 1.5418
DetectorType: SIEMENS / Details: COLLIMATOR / Detector: AREA DETECTOR / Collection date: Apr 14, 1992
RadiationMonochromator: GRAPHITE(002) / Monochromatic or laue m l: M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.5418 Å / Relative weight: 1
ReflectionNumber obs: 10591 / Observed criterion sigma I: 0 / Rmerge I obs: 0.083 / Redundancy: 0.98 % / Percent possible obs: 92

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Processing

Software
NameClassification
X-PLORmodel building
TNTrefinement
X-PLORrefinement
XENGENdata reduction
X-PLORphasing
RefineSigma F: 4
Least-squares processR factor R work: 0.19 / Highest resolution: 2.48 Å / Lowest resolution: 6 Å / Number reflection obs: 9538
Refine hist #LASTHighest resolution: 2.48 Å / Lowest resolution: 6 Å
Number of atoms included #LASTProtein: 2472 / Nucleic acid: 0 / Ligand: 0 / Solvent: 0 / Total: 2472
Refine LS restraints
Refine IDTypeDev idealWeight
X-RAY DIFFRACTIONt_bond_d0.0060.02
X-RAY DIFFRACTIONt_angle_deg2.13.0
X-RAY DIFFRACTIONt_dihedral_angle_d17.815.0
X-RAY DIFFRACTIONt_incorr_chiral_ct0
X-RAY DIFFRACTIONt_pseud_angle
X-RAY DIFFRACTIONt_trig_c_planes0.0040.020
X-RAY DIFFRACTIONt_gen_planes0.0080.020
X-RAY DIFFRACTIONt_it
X-RAY DIFFRACTIONt_nbd
Software
*PLUS
Name: TNT / Classification: refinement
Least-squares process
*PLUS
R factor obs: 0.19

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