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PDB: 4 results
4RZZ
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BU of 4rzz by Molmil
Crystal structure of metallopeptidase-like dimethylsulphoniopropionate (DMSP) lyase RlDddP in complex with phosphate
Descriptor: FE (III) ION, GLYCEROL, PHOSPHATE ION, ...
Authors:Zhang, Y, Wang, P.
Deposit date:2014-12-27
Release date:2015-08-05
Last modified:2024-02-28
Method:X-RAY DIFFRACTION (2.1 Å)
Cite:Structural and molecular basis for the novel catalytic mechanism and evolution of DddP, an abundant peptidase-like bacterial Dimethylsulfoniopropionate lyase: a new enzyme from an old fold.
Mol.Microbiol., 98, 2015
4S00
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BU of 4s00 by Molmil
Crystal structure of metallopeptidase-like dimethylsulphoniopropionate (DMSP) lyase RlDddP mutant Y366A in complex with acrylate
Descriptor: ACRYLIC ACID, FE (III) ION, GLYCEROL, ...
Authors:Zhang, Y, Wang, P.
Deposit date:2014-12-27
Release date:2015-08-05
Last modified:2024-02-28
Method:X-RAY DIFFRACTION (2.099 Å)
Cite:Structural and molecular basis for the novel catalytic mechanism and evolution of DddP, an abundant peptidase-like bacterial Dimethylsulfoniopropionate lyase: a new enzyme from an old fold.
Mol.Microbiol., 98, 2015
4RZY
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BU of 4rzy by Molmil
Crystal structure of metallopeptidase-like dimethylsulphoniopropionate (DMSP) lyase RlDddP in complex with MES
Descriptor: 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, FE (III) ION, Peptidase M24
Authors:Zhang, Y, Wang, P.
Deposit date:2014-12-26
Release date:2015-08-05
Last modified:2024-02-28
Method:X-RAY DIFFRACTION (1.949 Å)
Cite:Structural and molecular basis for the novel catalytic mechanism and evolution of DddP, an abundant peptidase-like bacterial Dimethylsulfoniopropionate lyase: a new enzyme from an old fold.
Mol.Microbiol., 98, 2015
4S01
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BU of 4s01 by Molmil
Crystal structure of metallopeptidase-like dimethylsulphoniopropionate (DMSP) lyase RlDddP mutant D377N in complex with acrylate
Descriptor: ACRYLIC ACID, FE (III) ION, GLYCEROL, ...
Authors:Zhang, Y, Wang, P.
Deposit date:2014-12-27
Release date:2015-08-05
Last modified:2024-02-28
Method:X-RAY DIFFRACTION (2.1 Å)
Cite:Structural and molecular basis for the novel catalytic mechanism and evolution of DddP, an abundant peptidase-like bacterial Dimethylsulfoniopropionate lyase: a new enzyme from an old fold.
Mol.Microbiol., 98, 2015

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