2I17

Human aldose reductase in complex with NADP+ and the inhibitor IDD594 at temperature of 60K

Summary for 2I17

• Entry DOI: 10.2210/pdb2i17/pdb
• Related: 1ADS 1AZ1 1AZ2 1EF3 1EL3 1IEI 1MAR 1US0 2ACQ 2I16
• Descriptor: Aldose reductase, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, IDD594, ... (5 entities in total)
• Functional Keywords: oxidoreductase, nadp, idd594, 60k
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: P15121
• Total number of polymer chains: 1
• Total formula weight: 37444.25

Authors

Petrova, T.,Ginell, S.,Mitshler, A.,Hasemann, I.,Schneider, T.,Cousido, A.,Lunin, V.Y.,Joachimiak, A.,Podjarny, A. (deposition date: 2006-08-13, release date: 2006-08-29, Last modification date: 2023-08-30)

Primary citation

Petrova, T.,Ginell, S.,Mitschler, A.,Hazemann, I.,Schneider, T.,Cousido, A.,Lunin, V.Y.,Joachimiak, A.,Podjarny, A.
Ultrahigh-resolution study of protein atomic displacement parameters at cryotemperatures obtained with a helium cryostat.
Acta Crystallogr.,Sect.D, 62:1535-1544, 2006

PubMed Abstract: Two X-ray data sets for a complex of human aldose reductase (h-AR) with the inhibitor IDD 594 and the cofactor NADP(+) were collected from two different parts of the same crystal to a resolution of 0.81 A at 15 and 60 K using cold helium gas as cryogen. The contribution of temperature to the atomic B values was estimated by comparison of the independently refined models. It was found that although being slightly different for different kinds of atoms, the differences (deltaB) in the isotropic equivalents B of atomic displacement parameters (ADPs) were approximately constant (about 1.7 A(2)) for well ordered atoms as the temperature was increased from 15 to 60 K. The mean value of this difference varied according to the number of non-H atoms covalently bound to the parent atom. Atoms having a B value of higher than 8 A(2) at 15 K showed much larger deviations of deltaB from the average value, which might reflect partial occupancy of atomic sites. An analysis of the anisotropy of ADPs for individual atoms revealed an increase in the isotropy of ADPs with the increase of the temperature from 15 to 60 K. In a separate experiment, a 0.93 A resolution data set was collected from a different crystal of the same complex at 100 K using cold nitrogen as a cryogen. The effects of various errors on the atomic B values were estimated by comparison of the refined models and the temperature-dependent component was inferred. It was found that both decreasing the data redundancy and increasing the resolution cutoff led to an approximately constant increase in atomic B values for well ordered atoms.

PubMed: 17139089
DOI: 10.1107/S0907444906041035

Experimental method

X-RAY DIFFRACTION (0.81 Å)