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- SASDF93: Ignicoccus islandicus malate dehydrogenase (Malate dehydrogenase) -

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Open data


ID or keywords:

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Basic information

Entry
Database: SASBDB / ID: SASDF93
SampleIgnicoccus islandicus malate dehydrogenase
  • Malate dehydrogenase (protein), Ignicoccus islandicus DSM 13165
Function / homology
Function and homology information


carboxylic acid metabolic process / oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Similarity search - Function
L-lactate/malate dehydrogenase / Lactate/malate dehydrogenase, N-terminal / Lactate/malate dehydrogenase, C-terminal / lactate/malate dehydrogenase, NAD binding domain / lactate/malate dehydrogenase, alpha/beta C-terminal domain / Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal / NAD(P)-binding domain superfamily
Similarity search - Domain/homology
Malate dehydrogenase
Similarity search - Component
Biological speciesIgnicoccus islandicus DSM 13165 (archaea)
CitationDate: 2019 Jul
Title: The archaeal LDH-like malate dehydrogenase from Ignicoccus islandicus displays dual substrate recognition, hidden allostery and a non-canonical tetrameric oligomeric organization
Authors: Roche J / Girard E / Mas C
Contact author
  • Jennifer Roche (IBS, Institut de Biologie Structurale, Grenoble, France)

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Models

Model #2822
Type: atomic / Chi-square value: 1.678
Search similar-shape structures of this assembly by Omokage search (details)

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Sample

SampleName: Ignicoccus islandicus malate dehydrogenase / Specimen concentration: 0.39-9.31
BufferName: 50 mM Tris-HCl 50 mM NaCl / pH: 7.4
Entity #1487Type: protein / Description: Malate dehydrogenase / Formula weight: 33.552 / Num. of mol.: 4 / Source: Ignicoccus islandicus DSM 13165 / References: UniProt: A0A0U3FQH7
Sequence: MARIPYKVAV IGTGRVGATF AYTMAVVPGI ARMTLVDVVP GLAKGVMEDI KHAAAVFRRS ITVEAFEDVS KVENADAIVI TAGKPRKADM SRRDLANVNA QIIRDIGDKL RDRNPGALYV VVTNPVDVMT MVLDDVIGSK GTVIGTGTSL DTFRFRAAVS ELLNVPIVAV ...Sequence:
MARIPYKVAV IGTGRVGATF AYTMAVVPGI ARMTLVDVVP GLAKGVMEDI KHAAAVFRRS ITVEAFEDVS KVENADAIVI TAGKPRKADM SRRDLANVNA QIIRDIGDKL RDRNPGALYV VVTNPVDVMT MVLDDVIGSK GTVIGTGTSL DTFRFRAAVS ELLNVPIVAV DGYVVGEHGE EAFVAWSTVT IKGIHIDQYI KERNINISRE QIEKYVKDVA ASIIASQGAT IWGPAATFQE IVVSHLANES KIIPISLPQN IEGVGRVAVS VPTIISGRLK PLVQLLNEEE QERLKRAAKA IRNVYESILT

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Experimental information

BeamInstrument name: ESRF BM29 / City: Grenoble / : France / Type of source: X-ray synchrotron / Wavelength: 0.125 Å / Dist. spec. to detc.: 2.85 mm
DetectorName: Pilatus 1M / Type: Dectris / Pixsize x: 172 mm
Scan
Title: Ignicoccus islandicus malate dehydrogenase / Measurement date: Sep 5, 2018 / Storage temperature: 20 °C / Cell temperature: 20 °C / Exposure time: 1 sec. / Number of frames: 10 / Unit: 1/nm /
MinMax
Q0.0447 4.9462
Distance distribution function P(R)
Sofotware P(R): GNOM 5.0 / Number of points: 391 /
MinMax
Q0.134376 1.9742
P(R) point1 391
R0 8.96
Result
Type of curve: merged /
ExperimentalPorod
MW118.75 kDa124 kDa
Volume-198 nm3

P(R)GuinierGuinier error
Forward scattering, I0107.7 109.12 0.61
Radius of gyration, Rg3.163 nm3.26 nm0.03

MinMax
D-8.96
Guinier point17 75

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