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1C52
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1c52
THERMUS THERMOPHILUS CYTOCHROME-C552: A NEW HIGHLY THERMOSTABLE CYTOCHROME-C STRUCTURE OBTAINED BY MAD PHASING
Descriptor:CYTOCHROME-C552, PROTOPORPHYRIN IX CONTAINING FE
Authors:Than, M.E., Hof, P., Huber, R., Bourenkov, G.P., Bartunik, H.D., Buse, G., Soulimane, T.
Deposit date:1997-06-23
Release date:1998-06-24
Modification date:2009-02-24
Method:X-RAY DIFFRACTION (1.28 Å)
Cite:Thermus thermophilus cytochrome-c552: A new highly thermostable cytochrome-c structure obtained by MAD phasing.
J.Mol.Biol., 271, 1997
1C53
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1c53
S-CLASS CYTOCHROMES C HAVE A VARIETY OF FOLDING PATTERNS: STRUCTURE OF CYTOCHROME C-553 FROM DESULFOVIBRIO VULGARIS DETERMINED BY THE MULTI-WAVELENGTH ANOMALOUS DISPERSION METHOD
Descriptor:CYTOCHROME C553
Authors:Nakagawa, A., Higuchi, Y., Yasuoka, N., Katsube, Y., Yaga, T.
Deposit date:1991-08-26
Release date:1993-10-31
Modification date:2009-02-24
Method:X-RAY DIFFRACTION (1.8 Å)
Cite:S-class cytochromes c have a variety of folding patterns: structure of cytochrome c-553 from Desulfovibrio vulgaris determined by the multi-wavelength anomalous dispersion method.
J.Biochem.(Tokyo), 108, 1990
1CCH
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1cch
THE SOLUTION CONFORMATION OF CYTOCHROME C-551 FROM P.STUTZERI ZOBELL DETERMINED BY NMR+
Descriptor:CYTOCHROME C551 (NMR, MINIMIZED AVERAGE STRUCTURE)
Authors:Cai, M., Timkovich, R.
Deposit date:1994-02-25
Release date:1994-04-30
Modification date:2009-02-24
Method:SOLUTION NMR
Cite:Investigation of the solution conformation of cytochrome c-551 from Pseudomonas stutzeri.
Biochemistry, 31, 1992
1CHH
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1chh
STRUCTURAL STUDIES OF THE ROLES OF RESIDUES 82 AND 85 AT THE INTERACTIVE FACE OF CYTOCHROME C
Descriptor:CYTOCHROME C (ISOZYME 1) (REDUCED) MUTANT WITH PHE 82 REPLACED BY TYR AND CYS 102 REPLACED BY THR (F82Y,C102T)
Authors:Lo, T.P., Brayer, G.D.
Deposit date:1994-06-01
Release date:1994-12-20
Modification date:2009-02-24
Method:X-RAY DIFFRACTION (1.97 Å)
Cite:Structural studies of the roles of residues 82 and 85 at the interactive face of cytochrome c.
Biochemistry, 34, 1995
1CHI
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1chi
STRUCTURAL STUDIES OF THE ROLES OF RESIDUES 82 AND 85 AT THE INTERACTIVE FACE OF CYTOCHROME C
Descriptor:CYTOCHROME C (ISOZYME 1) (REDUCED) MUTANT WITH PHE 82 REPLACED BY TYR, LEU 85 REPLACED BY ALA, AND CYS 102 REPLACED BY THR (F82Y,L85A,C102T)
Authors:Lo, T.P., Brayer, G.D.
Deposit date:1994-06-01
Release date:1994-12-20
Modification date:2009-02-24
Method:X-RAY DIFFRACTION (2 Å)
Cite:Structural studies of the roles of residues 82 and 85 at the interactive face of cytochrome c.
Biochemistry, 34, 1995
1CHJ
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1chj
STRUCTURAL STUDIES OF THE ROLES OF RESIDUES 82 AND 85 AT THE INTERACTIVE FACE OF CYTOCHROME C
Descriptor:CYTOCHROME C (ISOZYME 1) (REDUCED) MUTANT WITH LEU 85 REPLACED BY ALA AND CYS 102 REPLACED BY THR (L85A,C102T)
Authors:Lo, T.P., Brayer, G.D.
Deposit date:1994-06-01
Release date:1994-12-20
Modification date:2009-02-24
Method:X-RAY DIFFRACTION (1.9 Å)
Cite:Structural studies of the roles of residues 82 and 85 at the interactive face of cytochrome c.
Biochemistry, 34, 1995
1CIE
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1cie
STRUCTURAL AND FUNCTIONAL EFFECTS OF MULTIPLE MUTATIONS AT DISTAL SITES IN CYTOCHROME C
Descriptor:CYTOCHROME C (ISOZYME 1) (REDUCED) MUTANT WITH ASN 52 REPLACED BY ILE, PHE 82 REPLACED BY SER, AND CYS 102 REPLACED BY ALA (N52I,F82S,C102A)
Authors:Lo, T.P., Brayer, G.D.
Deposit date:1994-09-26
Release date:1995-01-26
Modification date:2009-02-24
Method:X-RAY DIFFRACTION (1.8 Å)
Cite:Structural and functional effects of multiple mutations at distal sites in cytochrome c.
Biochemistry, 34, 1995
1CIF
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1cif
STRUCTURAL AND FUNCTIONAL EFFECTS OF MULTIPLE MUTATIONS AT DISTAL SITES IN CYTOCHROME C
Descriptor:CYTOCHROME C (ISOZYME 1) (REDUCED) MUTANT WITH ARG 38 REPLACED BY ALA, PHE 82 REPLACED BY SER, AND CYS 102 REPLACED BY ALA (R38A,F82S,C102A)
Authors:Lo, T.P., Brayer, G.D.
Deposit date:1994-09-26
Release date:1995-01-26
Modification date:2009-02-24
Method:X-RAY DIFFRACTION (1.9 Å)
Cite:Structural and functional effects of multiple mutations at distal sites in cytochrome c.
Biochemistry, 34, 1995
1CIG
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1cig
STRUCTURAL AND FUNCTIONAL EFFECTS OF MULTIPLE MUTATIONS AT DISTAL SITES IN CYTOCHROME C
Descriptor:CYTOCHROME C (ISOZYME 1) (REDUCED) MUTANT WITH ARG 38 REPLACED BY ALA, ASN 52 REPLACED BY ILE, AND CYS 102 REPLACED BY ALA (R38A,N52I,C102A)
Authors:Lo, T.P., Brayer, G.D.
Deposit date:1994-09-26
Release date:1995-01-26
Modification date:2009-02-24
Method:X-RAY DIFFRACTION (1.8 Å)
Cite:Structural and functional effects of multiple mutations at distal sites in cytochrome c.
Biochemistry, 34, 1995
1CIH
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1cih
STRUCTURAL AND FUNCTIONAL EFFECTS OF MULTIPLE MUTATIONS AT DISTAL SITES IN CYTOCHROME C
Descriptor:CYTOCHROME C (ISOZYME 1) (REDUCED) MUTANT WITH ARG 38 REPLACED BY ALA, ASN 52 REPLACED BY ILE, PHE 82 REPLACED BY SER, AND CYS 102 REPLACED BY ALA (R38A,N52I,F82S,C102A)
Authors:Lo, T.P., Brayer, G.D.
Deposit date:1994-09-26
Release date:1995-01-26
Modification date:2009-02-24
Method:X-RAY DIFFRACTION (1.8 Å)
Cite:Structural and functional effects of multiple mutations at distal sites in cytochrome c.
Biochemistry, 34, 1995
1CO6
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1co6
CRYSTAL STRUCTURE OF FERROCYTOCHROME C2 FROM RHODOPSEUDOMONAS VIRIDIS
Descriptor:CYTOCHROME C2
Authors:Miki, K., Sogabe, S.
Deposit date:1999-06-05
Release date:1999-06-18
Modification date:2009-02-24
Method:X-RAY DIFFRACTION (1.6 Å)
Cite:Refined crystal structure of ferrocytochrome c2 from Rhodopseudomonas viridis at 1.6 A resolution.
J.Mol.Biol., 252, 1995
1CRG
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1crg
THE ROLE OF A CONSERVED INTERNAL WATER MOLECULE AND ITS ASSOCIATED HYDROGEN BOND NETWORK IN CYTOCHROME C
Descriptor:CYTOCHROME C (ISOZYME 1) (OXIDIZED) MUTANT WITH ASN 52 REPLACED BY ILE AND CYS 102 REPLACED BY THR (N52I,C102T)
Authors:Berghuis, A.M., Brayer, G.D.
Deposit date:1993-08-06
Release date:1994-01-31
Modification date:2009-02-24
Method:X-RAY DIFFRACTION (2 Å)
Cite:The role of a conserved internal water molecule and its associated hydrogen bond network in cytochrome c.
J.Mol.Biol., 236, 1994
1CRH
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1crh
THE ROLE OF A CONSERVED INTERNAL WATER MOLECULE AND ITS ASSOCIATED HYDROGEN BOND NETWORK IN CYTOCHROME C
Descriptor:CYTOCHROME C (ISOZYME 1) (REDUCED) MUTANT WITH ASN 52 REPLACED BY ILE (N52I)
Authors:Berghuis, A.M., Brayer, G.D.
Deposit date:1993-08-06
Release date:1994-01-31
Modification date:2009-02-24
Method:X-RAY DIFFRACTION (1.9 Å)
Cite:The role of a conserved internal water molecule and its associated hydrogen bond network in cytochrome c.
J.Mol.Biol., 236, 1994
1CRI
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1cri
THE ROLE OF A CONSERVED INTERNAL WATER MOLECULE AND ITS ASSOCIATED HYDROGEN BOND NETWORK IN CYTOCHROME C
Descriptor:CYTOCHROME C (ISOZYME 1) (OXIDIZED) MUTANT WITH ASN 52 REPLACED BY ILE, TYR 67 REPLACED BY PHE, AND CYS 102 REPLACED BY THR (N52I,Y67F,C102T)
Authors:Berghuis, A.M., Brayer, G.D.
Deposit date:1993-08-06
Release date:1994-01-31
Modification date:2009-02-24
Method:X-RAY DIFFRACTION (2 Å)
Cite:The role of a conserved internal water molecule and its associated hydrogen bond network in cytochrome c.
J.Mol.Biol., 236, 1994
1CRJ
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1crj
THE ROLE OF A CONSERVED INTERNAL WATER MOLECULE AND ITS ASSOCIATED HYDROGEN BOND NETWORK IN CYTOCHROME C
Descriptor:CYTOCHROME C (ISOZYME 1) (REDUCED) MUTANT WITH ASN 52 REPLACED BY ILE, TYR 67 REPLACED BY PHE, AND CYS 102 REPLACED BY THR (N52I,Y67F,C102T)
Authors:Berghuis, A.M., Brayer, G.D.
Deposit date:1993-08-06
Release date:1994-01-31
Modification date:2009-02-24
Method:X-RAY DIFFRACTION (2.05 Å)
Cite:The role of a conserved internal water molecule and its associated hydrogen bond network in cytochrome c.
J.Mol.Biol., 236, 1994
1CRY
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1cry
APPLICATION OF AN AUTOMATIC MOLECULAR REPLACEMENT PROCEDURE TO CRYSTAL STRUCTURE OF CYTOCHROME C2 FROM RHODOPSEUDOMONAS VIRIDIS
Descriptor:CYTOCHROME C2
Authors:Miki, K., Sogabe, S.
Deposit date:1993-12-27
Release date:1994-04-30
Modification date:2009-02-24
Method:X-RAY DIFFRACTION (3 Å)
Cite:Application of an automatic molecular-replacement procedure to crystal structure analysis of cytochrome c2 from Rhodopseudomonas viridis.
Acta Crystallogr.,Sect.D, 50, 1994
1CSU
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1csu
REPLACEMENTS IN A CONSERVED LEUCINE CLUSTER IN THE HYDROPHOBIC HEME POCKET OF CYTOCHROME C
Descriptor:CYTOCHROME C (ISOZYME 1) (REDUCED) MUTANT WITH LEU 85 REPLACED BY CYS AND CYS 102 REPLACED BY THR (L85C,C102T)
Authors:Lo, T.P., Brayer, G.D.
Deposit date:1994-10-04
Release date:1995-01-26
Modification date:2009-02-24
Method:X-RAY DIFFRACTION (1.81 Å)
Cite:Replacements in a conserved leucine cluster in the hydrophobic heme pocket of cytochrome c.
Protein Sci., 4, 1995
1CSV
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1csv
REPLACEMENTS IN A CONSERVED LEUCINE CLUSTER IN THE HYDROPHOBIC HEME POCKET OF CYTOCHROME C
Descriptor:CYTOCHROME C (ISOZYME 1) (REDUCED) MUTANT WITH LEU 85 REPLACED BY PHE AND CYS 102 REPLACED BY THR (L85F,C102T)
Authors:Lo, T.P., Brayer, G.D.
Deposit date:1994-10-04
Release date:1995-01-26
Modification date:2009-02-24
Method:X-RAY DIFFRACTION (1.9 Å)
Cite:Replacements in a conserved leucine cluster in the hydrophobic heme pocket of cytochrome c.
Protein Sci., 4, 1995
1CSW
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1csw
REPLACEMENTS IN A CONSERVED LEUCINE CLUSTER IN THE HYDROPHOBIC HEME POCKET OF CYTOCHROME C
Descriptor:CYTOCHROME C (ISOZYME 1) (REDUCED) MUTANT WITH LEU 85 REPLACED BY MET AND CYS 102 REPLACED BY THR (L85M,C102T)
Authors:Lo, T.P., Brayer, G.D.
Deposit date:1994-10-04
Release date:1995-01-26
Modification date:2009-02-24
Method:X-RAY DIFFRACTION (1.9 Å)
Cite:Replacements in a conserved leucine cluster in the hydrophobic heme pocket of cytochrome c.
Protein Sci., 4, 1995
1CSX
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1csx
REPLACEMENTS IN A CONSERVED LEUCINE CLUSTER IN THE HYDROPHOBIC HEME POCKET OF CYTOCHROME C
Descriptor:CYTOCHROME C (ISOZYME 1) (REDUCED) MUTANT WITH LEU 94 REPLACED BY SER AND CYS 102 REPLACED BY THR (L94S,C102T)
Authors:Lo, T.P., Brayer, G.D.
Deposit date:1994-10-04
Release date:1995-01-26
Modification date:2009-02-24
Method:X-RAY DIFFRACTION (1.9 Å)
Cite:Replacements in a conserved leucine cluster in the hydrophobic heme pocket of cytochrome c.
Protein Sci., 4, 1995
1CTY
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1cty
MUTATION OF TYROSINE-67 IN CYTOCHROME C SIGNIFICANTLY ALTERS THE LOCAL HEME ENVIRONMENT
Descriptor:CYTOCHROME C (ISOZYME 1) (OXIDIZED) MUTANT WITH TYR 67 REPLACED BY PHE AND CYS 102 REPLACED BY THR (Y67F, C102T)
Authors:Berghuis, A.M., Brayer, G.D.
Deposit date:1993-02-15
Release date:1993-07-15
Modification date:2009-02-24
Method:X-RAY DIFFRACTION (2.2 Å)
Cite:Mutation of tyrosine-67 to phenylalanine in cytochrome c significantly alters the local heme environment.
J.Mol.Biol., 235, 1994
1CTZ
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1ctz
MUTATION OF TYROSINE-67 IN CYTOCHROME C SIGNIFICANTLY ALTERS THE LOCAL HEME ENVIRONMENT
Descriptor:CYTOCHROME C (ISOZYME 1) (REDUCED) MUTANT WITH TYR 67 REPLACED BY PHE AND CYS 102 REPLACED BY THR (Y67F, C102T)
Authors:Berghuis, A.M., Brayer, G.D.
Deposit date:1993-02-15
Release date:1993-07-15
Modification date:2009-02-24
Method:X-RAY DIFFRACTION (1.9 Å)
Cite:Mutation of tyrosine-67 to phenylalanine in cytochrome c significantly alters the local heme environment.
J.Mol.Biol., 235, 1994
1DT1
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1dt1
THERMUS THERMOPHILUS CYTOCHROME C552 SYNTHESIZED BY ESCHERICHIA COLI
Descriptor:CYTOCHROME C552
Authors:Fee, J.A., Chen, Y., Hill, M.J., Gomez-Moran, E., Loehr, T., Ai, J., Thony-Meyer, L., Williams, P.A., Stura, E., Sridhar, V., McRee, D.E.
Deposit date:2000-01-10
Release date:2000-02-18
Modification date:2011-07-13
Method:X-RAY DIFFRACTION (1.8 Å)
Cite:Integrity of thermus thermophilus cytochrome c552 synthesized by Escherichia coli cells expressing the host-specific cytochrome c maturation genes, ccmABCDEFGH: biochemical, spectral, and structural characterization of the recombinant protein.
Protein Sci., 9, 2000
1DVH
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1dvh
STRUCTURE AND DYNAMICS OF FERROCYTOCHROME C553 FROM DESULFOVIBRIO VULGARIS STUDIED BY NMR SPECTROSCOPY AND RESTRAINED MOLECULAR DYNAMICS
Descriptor:CYTOCHROME C553 (REDUCED) (NMR, 36 STRUCTURES)
Authors:Blackledge, M.J., Medvedeva, S., Poncin, M., Guerlesquin, F., Bruschi, M., Marion, D.
Deposit date:1995-02-24
Release date:1995-06-03
Modification date:2009-02-24
Method:SOLUTION NMR
Cite:Structure and dynamics of ferrocytochrome c553 from Desulfovibrio vulgaris studied by NMR spectroscopy and restrained molecular dynamics.
J.Mol.Biol., 245, 1995
1FHB
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1fhb
THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE CYANIDE ADDUCT OF A MET80ALA VARIANT OF SACCHAROMYCES CEREVISIAE ISO-1-CYTOCHROME C. IDENTIFICATION OF LIGAND-RESIDUE INTERACTIONS IN THE DISTAL HEME CAVITY
Descriptor:FERRICYTOCHROME C, PROTOPORPHYRIN IX CONTAINING FE, METHYL PART OF N-TRIMETHYLLYSINE
Authors:Banci, L., Bertini, I., Bren, K.L., Gray, H.B., Sompornpisut, P., Turano, P.
Deposit date:1995-06-16
Release date:1995-09-15
Modification date:2009-02-24
Method:SOLUTION NMR
Cite:Three-Dimensional Solution Structure of the Cyanide Adduct of a met80Ala Variant of Saccharomyces Cerevisiae Iso-1-Cytochrome C. Identification of Ligand-Residue Interactions in the Distal Heme Cavity
Biochemistry, 34, 1995
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103354
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