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1DXO
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BU of 1dxo by Molmil
Crystal structure of human NAD[P]H-QUINONE oxidoreductase CO with 2,3,5,6,tetramethyl-P-benzoquinone (duroquinone) at 2.5 Angstrom resolution
Descriptor: DUROQUINONE, FLAVIN-ADENINE DINUCLEOTIDE, QUINONE REDUCTASE
Authors:Faig, M, Bianchet, M.A, Chen, S, Winski, S, Ross, D, Amzel, L.M.
Deposit date:2000-01-12
Release date:2000-04-23
Last modified:2017-07-05
Method:X-RAY DIFFRACTION (2.5 Å)
Cite:Structures of Recombinant Mouse and Human Nad(P)H:Quinone Oxidoreductases:Species Comparison and Structural Changes with Substrate Binding and Release
Proc.Natl.Acad.Sci.USA, 97, 2000
1NX8
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Structure of carbapenem synthase (CarC) complexed with N-acetyl proline
Descriptor: 1-ACETYL-L-PROLINE, 2-OXOGLUTARIC ACID, Carbapenem synthase, ...
Authors:Clifton, I.J, Doan, L.X, Sleeman, M.C, Topf, M, Suzuki, H, Wilmouth, R.C, Schofield, C.J.
Deposit date:2003-02-10
Release date:2003-06-17
Last modified:2023-08-16
Method:X-RAY DIFFRACTION (2.3 Å)
Cite:Crystal structure of carbapenem synthase (CarC).
J.Biol.Chem., 278, 2003
1D4A
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BU of 1d4a by Molmil
CRYSTAL STRUCTURE OF HUMAN NAD[P]H-QUINONE OXIDOREDUCTASE AT 1.7 A RESOLUTION
Descriptor: FLAVIN-ADENINE DINUCLEOTIDE, QUINONE REDUCTASE
Authors:Faig, M, Bianchet, M.A, Chen, S, Winski, S, Ross, D, Amzel, L.M.
Deposit date:1999-10-01
Release date:1999-10-15
Last modified:2024-02-07
Method:X-RAY DIFFRACTION (1.7 Å)
Cite:Structures of recombinant human and mouse NAD(P)H:quinone oxidoreductases: species comparison and structural changes with substrate binding and release.
Proc.Natl.Acad.Sci.USA, 97, 2000
1MDR
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BU of 1mdr by Molmil
THE ROLE OF LYSINE 166 IN THE MECHANISM OF MANDELATE RACEMASE FROM PSEUDOMONAS PUTIDA: MECHANISTIC AND CRYSTALLOGRAPHIC EVIDENCE FOR STEREOSPECIFIC ALKYLATION BY (R)-ALPHA-PHENYLGLYCIDATE
Descriptor: ATROLACTIC ACID (2-PHENYL-LACTIC ACID), MAGNESIUM ION, MANDELATE RACEMASE
Authors:Landro, J.A, Gerlt, J.A, Kozarich, J.W, Koo, C.W, Shah, V.J, Kenyon, G.L, Neidhart, D.J, Fujita, S, Petsko, G.A.
Deposit date:1993-11-19
Release date:1994-08-31
Last modified:2024-02-14
Method:X-RAY DIFFRACTION (2.1 Å)
Cite:The role of lysine 166 in the mechanism of mandelate racemase from Pseudomonas putida: mechanistic and crystallographic evidence for stereospecific alkylation by (R)-alpha-phenylglycidate.
Biochemistry, 33, 1994
1NX4
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The crystal structure of carbapenem synthase (CarC)
Descriptor: 2-OXOGLUTARIC ACID, Carbapenem synthase, FE (III) ION
Authors:Clifton, I.J, Doan, L.X, Sleeman, M.C, Topf, M, Suzuki, H, Wilmouth, R.C, Schofield, C.J.
Deposit date:2003-02-08
Release date:2003-06-17
Last modified:2011-07-13
Method:X-RAY DIFFRACTION (2.4 Å)
Cite:Crystal structure of carbapenem synthase (CarC).
J.Biol.Chem., 278, 2003
3NBJ
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Crystal Structure of Y305F mutant of the copper amine oxidase from Hansenula polymorpha expressed in yeast
Descriptor: COPPER (II) ION, PHOSPHATE ION, Peroxisomal primary amine oxidase
Authors:Chen, Z, Datta, S, DuBois, J.L, Klinman, J.P, Mathews, F.S.
Deposit date:2010-06-03
Release date:2010-08-25
Last modified:2023-11-22
Method:X-RAY DIFFRACTION (1.9 Å)
Cite:Mutation at a strictly conserved, active site tyrosine in the copper amine oxidase leads to uncontrolled oxygenase activity.
Biochemistry, 49, 2010
3N9H
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Crystal Structural of mutant Y305A in the copper amine oxidase from hansenula polymorpha
Descriptor: COPPER (II) ION, Peroxisomal primary amine oxidase
Authors:Chen, Z, Datta, S, DuBois, J.L, Klinman, J.P, Mathews, F.S.
Deposit date:2010-05-30
Release date:2010-08-25
Last modified:2023-09-06
Method:X-RAY DIFFRACTION (2.5 Å)
Cite:Mutation at a strictly conserved, active site tyrosine in the copper amine oxidase leads to uncontrolled oxygenase activity.
Biochemistry, 49, 2010
3NBB
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Crystal structure of mutant Y305F expressed in E. coli in the copper amine oxidase from hansenula polymorpha
Descriptor: COPPER (II) ION, Peroxisomal primary amine oxidase
Authors:Chen, Z, Datta, S, DuBois, J.L, Klinman, J.P, Mathews, F.S.
Deposit date:2010-06-03
Release date:2010-08-25
Last modified:2023-11-22
Method:X-RAY DIFFRACTION (2.05 Å)
Cite:Mutation at a strictly conserved, active site tyrosine in the copper amine oxidase leads to uncontrolled oxygenase activity.
Biochemistry, 49, 2010

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