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- PDB-1abn: THE CRYSTAL STRUCTURE OF THE ALDOSE REDUCTASE NADPH BINARY COMPLEX -

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Basic information

Entry
Database: PDB / ID: 1abn
TitleTHE CRYSTAL STRUCTURE OF THE ALDOSE REDUCTASE NADPH BINARY COMPLEX
ComponentsALDOSE REDUCTASE
KeywordsOXIDOREDUCTASE
Function / homology
Function and homology information


glyceraldehyde oxidoreductase activity / Fructose biosynthesis / fructose biosynthetic process / L-glucuronate reductase activity / aldose reductase / D/L-glyceraldehyde reductase / glycerol dehydrogenase (NADP+) activity / C21-steroid hormone biosynthetic process / NADP-retinol dehydrogenase / Pregnenolone biosynthesis ...glyceraldehyde oxidoreductase activity / Fructose biosynthesis / fructose biosynthetic process / L-glucuronate reductase activity / aldose reductase / D/L-glyceraldehyde reductase / glycerol dehydrogenase (NADP+) activity / C21-steroid hormone biosynthetic process / NADP-retinol dehydrogenase / Pregnenolone biosynthesis / allyl-alcohol dehydrogenase / allyl-alcohol dehydrogenase activity / prostaglandin H2 endoperoxidase reductase activity / regulation of urine volume / metanephric collecting duct development / all-trans-retinol dehydrogenase (NADP+) activity / daunorubicin metabolic process / doxorubicin metabolic process / retinal dehydrogenase (NAD+) activity / aldose reductase (NADPH) activity / epithelial cell maturation / cellular hyperosmotic salinity response / renal water homeostasis / retinoid metabolic process / carbohydrate metabolic process / electron transfer activity / negative regulation of apoptotic process / mitochondrion / extracellular space / extracellular exosome / nucleoplasm / cytosol
Similarity search - Function
Aldo/keto reductase family putative active site signature. / Aldo/keto reductase family signature 1. / 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
Similarity search - Domain/homology
Chem-NDP / Aldo-keto reductase family 1 member B1
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / Resolution: 2.4 Å
AuthorsBorhani, D.W. / Harter, T.M. / Petrash, J.M.
Citation
Journal: J.Biol.Chem. / Year: 1992
Title: The crystal structure of the aldose reductase.NADPH binary complex.
Authors: Borhani, D.W. / Harter, T.M. / Petrash, J.M.
#1: Journal: To be Published
Title: Probing the Active Site of Aldose Reductase: Site-Directed Mutagenesis of Asp-43, Tyr-48, Lys-77, and His-110
Authors: Tarle, I. / Borhani, D.W. / Wilson, D.K. / Quiocho, F.A. / Petrash, J.M.
#2: Journal: To be Published
Title: Studies on Pig Aldose Reductase: Identification of an Essential Arginine in the Primary and Tertiary Structure of the Enzyme
Authors: Kubiseski, T.J. / Green, N.C. / Borhani, D.W. / Flynn, T.G.
#3: Journal: Adv.Exp.Med.Biol. / Year: 1993
Title: Kinetic Alteration of Human Aldose Reductase by Mutagenesis of Cysteine Residues
Authors: Petrash, J.M. / Harter, T. / Tarle, I. / Borhani, D.
#4: Journal: J.Biol.Chem. / Year: 1992
Title: Involvement of Cysteine Residues in Catalysis and Inhibition of Human Aldose Reductase: Site Directed Mutagenesis of Cys-80,-298 and-303
Authors: Petrash, J.M. / Harter, T.M. / Devine, C.S. / Olins, P.O. / Bhatnagar, A. / Liu, S. / Srivastava, S.K.
History
DepositionSep 3, 1992Processing site: BNL
Revision 1.0Jan 31, 1994Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Nov 29, 2017Group: Derived calculations / Other
Category: pdbx_database_status / struct_conf / struct_conf_type
Item: _pdbx_database_status.process_site
Revision 1.4Feb 7, 2024Group: Data collection / Database references / Derived calculations
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: ALDOSE REDUCTASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)36,4972
Polymers35,7511
Non-polymers7451
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)74.710, 85.320, 106.840
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number23
Space group name H-MI222

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Components

#1: Protein ALDOSE REDUCTASE / Coordinate model: Cα atoms only


Mass: 35751.082 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli (E. coli) / References: UniProt: P15121, aldose reductase
#2: Chemical ChemComp-NDP / NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE


Mass: 745.421 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C21H30N7O17P3

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 2.38 Å3/Da / Density % sol: 48.31 %
Crystal grow
*PLUS
Temperature: 4 ℃ / pH: 6.2 / Method: vapor diffusion, hanging drop
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-IDChemical formula
110 mg/mlALR2:C298S1drop
225 mMMES1drop
31 mMdithiothreitol1drop
40.1 mMEDTA1drop
50.01 %1dropNaN3
649 mMNADPH in H2O1drop
76-13 %PEG60001drop
825 mMMES1drop
90.1 M1reservoirNaCl
10100 mMMES1reservoir

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Data collection

Reflection
*PLUS
Highest resolution: 2.2 Å

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Processing

Software
NameClassification
CORELSrefinement
TNTrefinement
RefinementResolution: 2.4→6 Å / Rfactor obs: 0.286
Refinement stepCycle: LAST / Resolution: 2.4→6 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms301 0 48 0 349
Refine LS restraints
*PLUS
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONo_bond_d0.022
X-RAY DIFFRACTIONo_angle_deg3.85

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