1A56
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PRIMARY SEQUENCE AND SOLUTION CONFORMATION OF FERRICYTOCHROME C-552 FROM NITROSOMONAS EUROPAEA, NMR, MEAN STRUCTURE REFINED WITH EXPLICIT HYDROGEN BOND CONSTRAINTS
Descriptor:FERRICYTOCHROME C-552, HEME C
Authors:Timkovich, R., Bergmann, D., Arciero, D.M., Hooper, A.B.
Deposit date:1998-02-20
Release date:1998-10-21
Modification date:2009-02-24
Method:SOLUTION NMR
Cite:Primary sequence and solution conformation of ferrocytochrome c-552 from Nitrosomonas europaea.
Biophys.J., 75, 1998
1A8C
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PRIMARY SEQUENCE AND SOLUTION CONFORMATION OF FERROCYTOCHROME C-552 FROM NITROSOMONAS EUROPAEA, NMR, MEAN STRUCTURE REFINED WITHOUT HYDROGEN BOND CONSTRAINTS
Descriptor:FERROCYTOCHROME C-552, HEME C
Authors:Timkovich, R., Bergmann, D., Arciero, D.M., Hooper, A.B.
Deposit date:1998-03-23
Release date:1998-10-21
Modification date:2009-02-24
Method:SOLUTION NMR
Cite:Primary sequence and solution conformation of ferrocytochrome c-552 from Nitrosomonas europaea.
Biophys.J., 75, 1998
1AKK
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SOLUTION STRUCTURE OF OXIDIZED HORSE HEART CYTOCHROME C, NMR, MINIMIZED AVERAGE STRUCTURE
Descriptor:CYTOCHROME C, HEME C
Authors:Banci, L., Bertini, I., Gray, H.B., Luchinat, C., Reddig, T., Rosato, A., Turano, P.
Deposit date:1997-05-22
Release date:1997-09-17
Modification date:2009-02-24
Method:SOLUTION NMR
Cite:Solution structure of oxidized horse heart cytochrome c.
Biochemistry, 36, 1997
1AYG
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SOLUTION STRUCTURE OF CYTOCHROME C-552, NMR, 20 STRUCTURES
Descriptor:CYTOCHROME C-552, HEME C
Authors:Hasegawa, J., Yoshida, T., Yamazaki, T., Sambongi, Y., Yu, Y., Igarashi, Y., Kodama, T., Yamazaki, K., Hakusui, H., Kyogoku, Y., Kobayashi, Y.
Deposit date:1997-11-04
Release date:1998-11-25
Modification date:2009-02-24
Method:SOLUTION NMR
Cite:Solution structure of thermostable cytochrome c-552 from Hydrogenobacter thermophilus determined by 1H-NMR spectroscopy.
Biochemistry, 37, 1998
1CCR
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STRUCTURE OF RICE FERRICYTOCHROME C AT 2.0 ANGSTROMS RESOLUTION
Descriptor:CYTOCHROME C
Authors:Ochi, H., Hata, Y., Tanaka, N., Kakudo, M., Sakurai, T., Aihara, S., Morita, Y.
Deposit date:1983-03-14
Release date:1983-04-21
Modification date:2009-02-24
Method:X-RAY DIFFRACTION (1.5 Å)
Cite:Structure of rice ferricytochrome c at 2.0 A resolution.
J.Mol.Biol., 166, 1983
1CHH
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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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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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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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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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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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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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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
1CRC
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CYTOCHROME C AT LOW IONIC STRENGTH
Descriptor:CYTOCHROME C, PROTOPORPHYRIN IX CONTAINING FE
Authors:Sanishvili, R., Volz, K.W., Westbrook, E.M., Margoliash, E.
Deposit date:1995-03-22
Release date:1996-03-08
Modification date:2009-02-24
Method:X-RAY DIFFRACTION (2.08 Å)
Cite:The low ionic strength crystal structure of horse cytochrome c at 2.1 A resolution and comparison with its high ionic strength counterpart.
Structure, 3, 1995
1CRG
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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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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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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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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
1CSU
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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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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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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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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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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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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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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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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
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