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PDB: 15 results

1TUM
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BU of 1tum by Molmil
MUTT PYROPHOSPHOHYDROLASE-METAL-NUCLEOTIDE-METAL COMPLEX, NMR, 16 STRUCTURES
Descriptor: COBALT TETRAAMMINE ION, DIPHOSPHOMETHYLPHOSPHONIC ACID ADENOSYL ESTER, MAGNESIUM ION, ...
Authors:Lin, J, Abeygunawardana, C, Frick, D.N, Bessman, M.J, Mildvan, A.S.
Deposit date:1996-12-05
Release date:1997-05-15
Last modified:2024-05-22
Method:SOLUTION NMR
Cite:Solution structure of the quaternary MutT-M2+-AMPCPP-M2+ complex and mechanism of its pyrophosphohydrolase action.
Biochemistry, 36, 1997
1PPX
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Solution Structure of the MutT Pyrophosphohydrolase Complexed with Mg(2+) and 8-oxo-dGMP, a Tightly-bound Product
Descriptor: 8-OXO-2'-DEOXY-GUANOSINE-5'-MONOPHOSPHATE, MAGNESIUM ION, Mutator mutT protein
Authors:Massiah, M.A, Saraswat, V, Azurmendi, H.F, Mildvan, A.S.
Deposit date:2003-06-17
Release date:2003-08-26
Last modified:2024-05-22
Method:SOLUTION NMR
Cite:Solution structure and NH exchange studies of the MutT pyrophosphohydrolase complexed with Mg(2+) and 8-oxo-dGMP, a tightly bound product.
Biochemistry, 42, 2003
1PUN
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Solution Structure of the MutT Pyrophosphohydrolase Complexed with Mg(2+) and 8-oxo-dGMP, a Tightly-bound Product
Descriptor: 8-OXO-2'-DEOXY-GUANOSINE-5'-MONOPHOSPHATE, MAGNESIUM ION, Mutator mutT protein
Authors:Massiah, M.A, Saraswat, V, Azurmendi, H.F, Mildvan, A.S.
Deposit date:2003-06-25
Release date:2003-08-26
Last modified:2024-05-22
Method:SOLUTION NMR
Cite:Solution structure and NH exchange studies of the MutT pyrophosphohydrolase complexed with Mg(2+) and 8-oxo-dGMP, a tightly bound product.
Biochemistry, 42, 2003
1PUQ
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Solution Structure of the MutT Pyrophosphohydrolase Complexed with Mg(2+) and 8-oxo-dGMP, a Tightly-bound Product
Descriptor: 8-OXO-2'-DEOXY-GUANOSINE-5'-MONOPHOSPHATE, MAGNESIUM ION, Mutator mutT protein
Authors:Massiah, M.A, Saraswat, V, Azurmendi, H.F, Mildvan, A.S.
Deposit date:2003-06-25
Release date:2003-08-26
Last modified:2024-05-01
Method:SOLUTION NMR
Cite:Solution structure and NH exchange studies of the MutT pyrophosphohydrolase complexed with Mg(2+) and 8-oxo-dGMP, a tightly bound product.
Biochemistry, 42, 2003
1PUS
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Solution Structure of the MutT Pyrophosphohydrolase Complexed with Mg(2+) and 8-oxo-dGMP, a Tightly-bound Product
Descriptor: 8-OXO-2'-DEOXY-GUANOSINE-5'-MONOPHOSPHATE, MAGNESIUM ION, Mutator mutT protein
Authors:Massiah, M.A, Saraswat, V, Azurmendi, H.F, Mildvan, A.S.
Deposit date:2003-06-25
Release date:2003-08-26
Last modified:2024-05-01
Method:SOLUTION NMR
Cite:Solution structure and NH exchange studies of the MutT pyrophosphohydrolase complexed with Mg(2+) and 8-oxo-dGMP, a tightly bound product.
Biochemistry, 42, 2003
1IK4
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BU of 1ik4 by Molmil
X-ray Structure of Methylglyoxal Synthase from E. coli Complexed with Phosphoglycolohydroxamic Acid
Descriptor: METHYLGLYOXAL SYNTHASE, PHOSPHOGLYCOLOHYDROXAMIC ACID
Authors:Marks, G.T, Harris, T.K, Massiah, M.A, Mildvan, A.S, Harrison, D.H.T.
Deposit date:2001-05-02
Release date:2001-09-26
Last modified:2024-02-07
Method:X-RAY DIFFRACTION (2 Å)
Cite:Mechanistic implications of methylglyoxal synthase complexed with phosphoglycolohydroxamic acid as observed by X-ray crystallography and NMR spectroscopy.
Biochemistry, 40, 2001
1MUT
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NMR STUDY OF MUTT ENZYME, A NUCLEOSIDE TRIPHOSPHATE PYROPHOSPHOHYDROLASE
Descriptor: NUCLEOSIDE TRIPHOSPHATE PYROPHOSPHOHYDROLASE
Authors:Abeygunawardana, C, Weber, D.J, Gittis, A.G, Frick, D.N, Lin, J, Miller, A.-F, Bessman, M.J, Mildvan, A.S.
Deposit date:1995-09-14
Release date:1996-04-03
Last modified:2024-05-22
Method:SOLUTION NMR
Cite:Solution structure of the MutT enzyme, a nucleoside triphosphate pyrophosphohydrolase.
Biochemistry, 34, 1995
1RYA
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Crystal Structure of the E. coli GDP-mannose mannosyl hydrolase in complex with GDP and MG
Descriptor: 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, CHLORIDE ION, GDP-mannose mannosyl hydrolase, ...
Authors:Gabelli, S.B, Bianchet, M.A, Legler, P.M, Mildvan, A.S, Amzel, L.M.
Deposit date:2003-12-20
Release date:2004-06-22
Last modified:2024-02-14
Method:X-RAY DIFFRACTION (1.3 Å)
Cite:Structure and mechanism of GDP-mannose glycosyl hydrolase, a Nudix enzyme that cleaves at carbon instead of phosphorus.
Structure, 12, 2004
2GT4
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Crystal Structure of the Y103F mutant of the GDP-mannose mannosyl hydrolase in complex with GDP-mannose and MG+2
Descriptor: GDP-mannose mannosyl hydrolase, GUANOSINE-5'-DIPHOSPHATE-ALPHA-D-MANNOSE, MAGNESIUM ION, ...
Authors:Gabelli, S.B, Bianchet, M.A, Azurmendi, H.F, Mildvan, A.S, Amzel, L.A.
Deposit date:2006-04-27
Release date:2006-12-12
Last modified:2023-08-30
Method:X-RAY DIFFRACTION (2.3 Å)
Cite:X-ray, NMR, and mutational studies of the catalytic cycle of the GDP-mannose mannosyl hydrolase reaction.
Biochemistry, 45, 2006
2GT2
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Structure of the E. coli GDP-mannose mannosyl hydrolase
Descriptor: GDP-mannose mannosyl hydrolase
Authors:Gabelli, S.B, Bianchet, M.A, Azurmendi, H.F, MIldvan, A.S, Amzel, L.M.
Deposit date:2006-04-27
Release date:2006-12-12
Last modified:2023-08-30
Method:X-RAY DIFFRACTION (2 Å)
Cite:X-ray, NMR, and mutational studies of the catalytic cycle of the GDP-mannose mannosyl hydrolase reaction.
Biochemistry, 45, 2006
1BUQ
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SOLUTION STRUCTURE OF DELTA-5-3-KETOSTEROID ISOMERASE COMPLEXED WITH THE STEROID 19-NORTESTOSTERONE-HEMISUCCINATE
Descriptor: PROTEIN (3-KETOSTEROID ISOMERASE-19-NORTESTOSTERONE-HEMISUCCINATE), SUCCINIC ACID MONO-(13-METHYL-3-OXO-2,3,6,7,8,9,10,11,12,13,14,15,16,17-TETRADECAHYDRO-1H-CYCLOPENTA[A]PHENANTHREN-17-YL) ESTER
Authors:Massiah, M.A, Abeygunawardana, C, Gittis, A.G, Mildvan, A.S.
Deposit date:1998-09-04
Release date:1999-01-20
Last modified:2024-05-22
Method:SOLUTION NMR
Cite:Solution structure of Delta 5-3-ketosteroid isomerase complexed with the steroid 19-nortestosterone hemisuccinate.
Biochemistry, 37, 1998
1CKW
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CYSTIC FIBROSIS TRANSMEMBRANE CONDUCTANCE REGULATOR: SOLUTION STRUCTURES OF PEPTIDES BASED ON THE PHE508 REGION, THE MOST COMMON SITE OF DISEASE-CAUSING DELTA-F508 MUTATION
Descriptor: PROTEIN (CYSTIC FIBROSIS TRANSMEMBRANE CONDUCTANCE REGULATOR (CFTR))
Authors:Massiah, M.A, Ko, Y.H, Pedersen, P.L, Mildvan, A.S.
Deposit date:1999-04-26
Release date:1999-05-04
Last modified:2023-12-27
Method:SOLUTION NMR
Cite:Cystic fibrosis transmembrane conductance regulator: solution structures of peptides based on the Phe508 region, the most common site of disease-causing DeltaF508 mutation.
Biochemistry, 38, 1999
1CKZ
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BU of 1ckz by Molmil
CYSTIC FIBROSIS TRANSMEMBRANE CONDUCTANCE REGULATOR: SOLUTION STRUCTURES OF PEPTIDES BASED ON THE PHE508 REGION, THE MOST COMMON SITE OF DISEASE-CAUSING DELTA-F508 MUTATION
Descriptor: PROTEIN (CYSTIC FIBROSIS TRANSMEMBRANE CONDUCTANCE REGULATOR (CFTR))
Authors:Massiah, M.A, Ko, Y.H, Pedersen, P.L, Mildvan, A.S.
Deposit date:1999-04-26
Release date:1999-05-04
Last modified:2023-12-27
Method:SOLUTION NMR
Cite:Cystic fibrosis transmembrane conductance regulator: solution structures of peptides based on the Phe508 region, the most common site of disease-causing DeltaF508 mutation.
Biochemistry, 38, 1999
1CKX
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Cystic fibrosis transmembrane conductance regulator: Solution structures of peptides based on the Phe508 region, the most common site of disease-causing Delta-F508 mutation
Descriptor: Cystic fibrosis transmembrane conductance regulator (CFTR)
Authors:Massiah, M.A, Ko, Y.H, Pedersen, P.L, Mildvan, A.S.
Deposit date:1999-04-26
Release date:1999-05-04
Last modified:2023-12-27
Method:SOLUTION NMR
Cite:Cystic fibrosis transmembrane conductance regulator: solution structures of peptides based on the Phe508 region, the most common site of disease-causing DeltaF508 mutation.
Biochemistry, 38, 1999
1CKY
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BU of 1cky by Molmil
CYSTIC FIBROSIS TRANSMEMBRANE CONDUCTANCE REGULATOR: SOLUTION STRUCTURES OF PEPTIDES BASED ON THE PHE508 REGION, THE MOST COMMON SITE OF DISEASE-CAUSING DELTA-F508 MUTATION
Descriptor: PROTEIN (CYSTIC FIBROSIS TRANSMEMBRANE CONDUCTANCE REGULATOR (CFTR))
Authors:Massiah, M.A, Ko, Y.H, Pedersen, P.L, Mildvan, A.S.
Deposit date:1999-04-26
Release date:1999-05-04
Last modified:2023-12-27
Method:SOLUTION NMR
Cite:Cystic fibrosis transmembrane conductance regulator: solution structures of peptides based on the Phe508 region, the most common site of disease-causing DeltaF508 mutation.
Biochemistry, 38, 1999

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