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PDB: 7 results

3LIO
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BU of 3lio by Molmil
X-ray structure of the iron superoxide dismutase from pseudoalteromonas haloplanktis (crystal form I)
Descriptor: FE (III) ION, alpha-D-glucopyranose-(1-1)-alpha-D-glucopyranose, iron superoxide dismutase
Authors:Merlino, A, Russo Krauss, I, Rossi, B, Conte, M, Vergara, A, Sica, F.
Deposit date:2010-01-25
Release date:2010-09-08
Last modified:2023-09-06
Method:X-RAY DIFFRACTION (1.5 Å)
Cite:Structure and flexibility in cold-adapted iron superoxide dismutases: the case of the enzyme isolated from Pseudoalteromonas haloplanktis.
J.Struct.Biol., 172, 2010
4L2C
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BU of 4l2c by Molmil
X-ray structure of the C57R mutant of the iron superoxide dismutase from Pseudoalteromonas haloplanktis (crystal form I)
Descriptor: FE (III) ION, Superoxide dismutase [Fe], alpha-D-glucopyranose-(1-1)-alpha-D-glucopyranose
Authors:Russo Krauss, I, Merlino, A, Sica, F.
Deposit date:2013-06-04
Release date:2014-02-26
Last modified:2024-02-28
Method:X-RAY DIFFRACTION (1.66 Å)
Cite:Structural and denaturation studies of two mutants of a cold adapted superoxide dismutase point to the importance of electrostatic interactions in protein stability.
Biochim.Biophys.Acta, 1844, 2014
4L2B
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BU of 4l2b by Molmil
X-ray structure of the C57S mutant of the iron superoxide dismutase from Pseudoalteromonas haloplanktis
Descriptor: FE (III) ION, Superoxide dismutase [Fe], alpha-D-glucopyranose-(1-1)-alpha-D-glucopyranose
Authors:Merlino, A, Russo Krauss, I, Sica, F.
Deposit date:2013-06-04
Release date:2014-02-26
Last modified:2024-02-28
Method:X-RAY DIFFRACTION (1.97 Å)
Cite:Structural and denaturation studies of two mutants of a cold adapted superoxide dismutase point to the importance of electrostatic interactions in protein stability.
Biochim.Biophys.Acta, 1844, 2014
4L2A
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BU of 4l2a by Molmil
X-ray structure of the C57R mutant of the iron superoxide dismutase from Pseudoalteromonas haloplanktis (crystal form II)
Descriptor: FE (III) ION, Superoxide dismutase [Fe]
Authors:Merlino, A, Russo Krauss, I, Sica, F.
Deposit date:2013-06-04
Release date:2014-02-26
Last modified:2024-02-28
Method:X-RAY DIFFRACTION (2.06 Å)
Cite:Structural and denaturation studies of two mutants of a cold adapted superoxide dismutase point to the importance of electrostatic interactions in protein stability.
Biochim.Biophys.Acta, 1844, 2014
4L2D
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BU of 4l2d by Molmil
X-ray structure of the Fe(II) form of the iron superoxide dismutase from Pseudoalteromonas haloplanktis
Descriptor: FE (II) ION, Superoxide dismutase [Fe], alpha-D-glucopyranose-(1-1)-alpha-D-glucopyranose
Authors:Russo Krauss, I, Merlino, A, Sica, F.
Deposit date:2013-06-04
Release date:2014-02-26
Last modified:2024-02-28
Method:X-RAY DIFFRACTION (2.07 Å)
Cite:Structural and denaturation studies of two mutants of a cold adapted superoxide dismutase point to the importance of electrostatic interactions in protein stability.
Biochim.Biophys.Acta, 1844, 2014
3LJF
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BU of 3ljf by Molmil
The X-ray structure of iron superoxide dismutase from Pseudoalteromonas haloplanktis (crystal form II)
Descriptor: FE (III) ION, alpha-D-glucopyranose-(1-1)-alpha-D-glucopyranose, iron superoxide dismutase
Authors:Merlino, A, Russo Krauss, I, Rossi, B, Conte, M, Vergara, A, Sica, F.
Deposit date:2010-01-26
Release date:2010-09-08
Last modified:2023-09-06
Method:X-RAY DIFFRACTION (2.1 Å)
Cite:Structure and flexibility in cold-adapted iron superoxide dismutases: the case of the enzyme isolated from Pseudoalteromonas haloplanktis.
J.Struct.Biol., 172, 2010
3LJ9
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BU of 3lj9 by Molmil
X-ray structure of the iron superoxide dismutase from pseudoalteromonas haloplanktis in complex with sodium azide
Descriptor: AZIDE ION, FE (III) ION, alpha-D-glucopyranose-(1-1)-alpha-D-glucopyranose, ...
Authors:Merlino, A, Russo Krauss, I, Rossi, B, Conte, M, Vergara, A, Sica, F.
Deposit date:2010-01-26
Release date:2010-09-08
Last modified:2023-09-06
Method:X-RAY DIFFRACTION (2.1 Å)
Cite:Structure and flexibility in cold-adapted iron superoxide dismutases: the case of the enzyme isolated from Pseudoalteromonas haloplanktis.
J.Struct.Biol., 172, 2010

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