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PDB: 409 results

1LHJ
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ROLE OF PROLINE RESIDUES IN HUMAN LYSOZYME STABILITY: A SCANNING CALORIMETRIC STUDY COMBINED WITH X-RAY STRUCTURE ANALYSIS OF PROLINE MUTANTS
Descriptor: HUMAN LYSOZYME
Authors:Inaka, K, Matsushima, M, Herning, T, Kuroki, R, Yutani, K, Kikuchi, M.
Deposit date:1992-03-27
Release date:1994-01-31
Last modified:2017-11-29
Method:X-RAY DIFFRACTION (1.8 Å)
Cite:Role of proline residues in human lysozyme stability: a scanning calorimetric study combined with X-ray structure analysis of proline mutants.
Biochemistry, 31, 1992
7CBD
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BU of 7cbd by Molmil
Catalytic domain of Cellulomonas fimi Cel6B
Descriptor: Exoglucanase A
Authors:Nakamura, A, Ishiwata, D, Visootsat, A, Uchiyama, T, Mizutani, K, Kaneko, S, Murata, T, Igarashi, K, Iino, R.
Deposit date:2020-06-12
Release date:2020-08-26
Last modified:2023-11-29
Method:X-RAY DIFFRACTION (1.3 Å)
Cite:Domain architecture divergence leads to functional divergence in binding and catalytic domains of bacterial and fungal cellobiohydrolases.
J.Biol.Chem., 295, 2020
7DQE
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BU of 7dqe by Molmil
Crystal structure of the ADP-bound mutant A(S23C)3B(N64C)3 complex from enterococcus hirae V-ATPase
Descriptor: ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, SULFATE ION, ...
Authors:Maruyama, S, Nakamoto, K, Suzuki, K, Mizutani, K, Imai, F.L, Ishizuka-Katsura, Y, Shirouzu, M, Murata, T.
Deposit date:2020-12-23
Release date:2021-12-29
Last modified:2023-11-29
Method:X-RAY DIFFRACTION (2.694 Å)
Cite:The Combination of High-Speed AFM and X-ray Crystallography Reveals Rotary Catalytic Mechanism of Shaftless V1-ATPase
To Be Published
7DQD
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Crystal structure of the AMP-PNP-bound mutant A(S23C)3B(N64C)3 complex from enterococcus hirae V-ATPase
Descriptor: GLYCEROL, MAGNESIUM ION, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, ...
Authors:Maruyama, S, Suzuki, K, Mizutani, K, Imai, F.L, Ishizuka-Katsura, Y, Shirouzu, M, Murata, T.
Deposit date:2020-12-23
Release date:2021-12-29
Last modified:2023-11-29
Method:X-RAY DIFFRACTION (3.383 Å)
Cite:The combination of high-speed AFM and X-ray crystallography reveals rotary catalysis
To Be Published
7DQC
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BU of 7dqc by Molmil
Crystal structure of nucleotide-free mutant A(S23C)3B(N64C)3 complex from Enterococcus hirae V-ATPase
Descriptor: GLYCEROL, V-type sodium ATPase catalytic subunit A, V-type sodium ATPase subunit B
Authors:Maruyama, S, Suzuki, K, Mizutani, K, Imai, F.L, Ishizuka-Katsura, Y, Shirouzu, M, Murata, M.
Deposit date:2020-12-23
Release date:2021-12-29
Last modified:2023-11-29
Method:X-RAY DIFFRACTION (2.706 Å)
Cite:The combination of high-speed AFM and X-ray crystallography reveals rotary catalytic mechanism of shaftless V1-ATPase
To Be Published
6KJL
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Xylanase J from Bacillus sp. strain 41M-1
Descriptor: (4S)-2-METHYL-2,4-PENTANEDIOL, 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID, CALCIUM ION, ...
Authors:Manami, S, Teisuke, T, Nakatani, K, Katano, K, Kojima, K, Saka, N, Mikami, B, Yatsunami, R, Nakamura, S, Yasukawa, K.
Deposit date:2019-07-22
Release date:2019-09-04
Last modified:2023-11-22
Method:X-RAY DIFFRACTION (2.45 Å)
Cite:Increase in the thermostability of GH11 xylanase XynJ from Bacillus sp. strain 41M-1 using site saturation mutagenesis.
Enzyme.Microb.Technol., 130, 2019
1Z8W
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Structure of Mutant Pyrrolidone Carboxyl Peptidase (E192I) from a Hyperthermophile, Pyrococcus furiosus
Descriptor: Pyrrolidone-carboxylate peptidase
Authors:Kaushik, J.K, Yamagata, Y, Ogasahara, K, Yutani, K.
Deposit date:2005-03-31
Release date:2006-06-13
Last modified:2023-10-25
Method:X-RAY DIFFRACTION (2 Å)
Cite:Completely buried, non-ion-paired glutamic acid contributes favorably to the conformational stability of pyrrolidone carboxyl peptidases from hyperthermophiles.
Biochemistry, 45, 2006
1Z8X
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Structure of Mutant Pyrrolidone Carboxyl Peptidase (E192V) from a Hyperthermophile, Pyrococcus furiosus
Descriptor: Pyrrolidone-carboxylate peptidase
Authors:Kaushik, J.K, Yamagata, Y, Ogasahara, K, Yutani, K.
Deposit date:2005-03-31
Release date:2006-06-13
Last modified:2023-10-25
Method:X-RAY DIFFRACTION (2 Å)
Cite:Completely buried, non-ion-paired glutamic acid contributes favorably to the conformational stability of pyrrolidone carboxyl peptidases from hyperthermophiles.
Biochemistry, 45, 2006
1Z8T
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Structure of Mutant Pyrrolidone Carboxyl Peptidase (E192Q) from a Hyperthermophile, Pyrococcus furiosus
Descriptor: Pyrrolidone-carboxylate peptidase
Authors:Kaushik, J.K, Yamagata, Y, Ogasahara, K, Yutani, K.
Deposit date:2005-03-31
Release date:2006-06-13
Last modified:2023-10-25
Method:X-RAY DIFFRACTION (2.5 Å)
Cite:Completely buried, non-ion-paired glutamic acid contributes favorably to the conformational stability of pyrrolidone carboxyl peptidases from hyperthermophiles.
Biochemistry, 45, 2006
1IOC
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CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME, EAEA-I56T
Descriptor: LYSOZYME C, SODIUM ION
Authors:Goda, S, Takano, K, Yamagata, Y, Yutani, K.
Deposit date:2001-02-27
Release date:2002-10-09
Last modified:2024-04-03
Method:X-RAY DIFFRACTION (2.4 Å)
Cite:Elongation in a beta-structure promotes amyloid-like fibril formation of human lysozyme.
J.Biochem., 132, 2002
1GB6
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BU of 1gb6 by Molmil
CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS
Descriptor: LYSOZYME, SODIUM ION
Authors:Funahashi, J, Takano, K, Yamagata, Y, Yutani, K.
Deposit date:2000-06-26
Release date:2000-07-27
Last modified:2023-12-27
Method:X-RAY DIFFRACTION (1.8 Å)
Cite:Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions.
Biochemistry, 39, 2000
1GBY
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BU of 1gby by Molmil
CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS
Descriptor: LYSOZYME, SODIUM ION
Authors:Funahashi, J, Takano, K, Yamagata, Y, Yutani, K.
Deposit date:2000-06-26
Release date:2000-07-27
Last modified:2023-12-27
Method:X-RAY DIFFRACTION (1.8 Å)
Cite:Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions.
Biochemistry, 39, 2000
1GFH
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CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS
Descriptor: LYSOZYME, SODIUM ION
Authors:Funahashi, J, Takano, K, Yamagata, Y, Yutani, K.
Deposit date:2000-12-04
Release date:2000-12-20
Last modified:2023-12-27
Method:X-RAY DIFFRACTION (1.8 Å)
Cite:Positive contribution of hydration structure on the surface of human lysozyme to the conformational stability.
J.Biol.Chem., 277, 2002
1GDX
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BU of 1gdx by Molmil
CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT LEFT-HANDED HELICAL POSITIONS
Descriptor: LYSOZYME C, SODIUM ION
Authors:Takano, K, Yamagata, Y, Yutani, K.
Deposit date:2000-10-06
Release date:2000-11-08
Last modified:2023-12-27
Method:X-RAY DIFFRACTION (1.8 Å)
Cite:Role of non-glycine residues in left-handed helical conformation for the conformational stability of human lysozyme
Proteins, 44, 2001
1GFT
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BU of 1gft by Molmil
CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS
Descriptor: LYSOZYME, SODIUM ION
Authors:Funahashi, J, Takano, K, Yamagata, Y, Yutani, K.
Deposit date:2000-12-04
Release date:2000-12-27
Last modified:2023-12-27
Method:X-RAY DIFFRACTION (1.8 Å)
Cite:Positive contribution of hydration structure on the surface of human lysozyme to the conformational stability.
J.Biol.Chem., 277, 2002
1GE1
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BU of 1ge1 by Molmil
CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT LEFT-HANDED HELICAL POSITIONS
Descriptor: LYSOZYME C, SODIUM ION
Authors:Takano, K, Yamagata, Y, Yutani, K.
Deposit date:2000-10-06
Release date:2000-11-08
Last modified:2023-12-27
Method:X-RAY DIFFRACTION (1.7 Å)
Cite:Role of non-glycine residues in left-handed helical conformation for the conformational stability of human lysozyme
Proteins, 44, 2001
1LHH
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BU of 1lhh by Molmil
ROLE OF PROLINE RESIDUES IN HUMAN LYSOZYME STABILITY: A SCANNING CALORIMETRIC STUDY COMBINED WITH X-RAY STRUCTURE ANALYSIS OF PROLINE MUTANTS
Descriptor: HUMAN LYSOZYME
Authors:Inaka, K, Matsushima, M, Herning, T, Kuroki, R, Yutani, K, Kikuchi, M.
Deposit date:1992-03-27
Release date:1994-01-31
Last modified:2017-11-29
Method:X-RAY DIFFRACTION (1.8 Å)
Cite:Role of proline residues in human lysozyme stability: a scanning calorimetric study combined with X-ray structure analysis of proline mutants.
Biochemistry, 31, 1992
1LHK
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BU of 1lhk by Molmil
ROLE OF PROLINE RESIDUES IN HUMAN LYSOZYME STABILITY: A SCANNING CALORIMETRIC STUDY COMBINED WITH X-RAY STRUCTURE ANALYSIS OF PROLINE MUTANTS
Descriptor: HUMAN LYSOZYME
Authors:Inaka, K, Matsushima, M, Herning, T, Kuroki, R, Yutani, K, Kikuchi, M.
Deposit date:1992-03-27
Release date:1994-01-31
Last modified:2017-11-29
Method:X-RAY DIFFRACTION (1.8 Å)
Cite:Role of proline residues in human lysozyme stability: a scanning calorimetric study combined with X-ray structure analysis of proline mutants.
Biochemistry, 31, 1992
1LHL
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BU of 1lhl by Molmil
ROLE OF PROLINE RESIDUES IN HUMAN LYSOZYME STABILITY: A SCANNING CALORIMETRIC STUDY COMBINED WITH X-RAY STRUCTURE ANALYSIS OF PROLINE MUTANTS
Descriptor: HUMAN LYSOZYME
Authors:Inaka, K, Matsushima, M, Herning, T, Kuroki, R, Yutani, K, Kikuchi, M.
Deposit date:1992-03-27
Release date:1994-01-31
Last modified:2017-11-29
Method:X-RAY DIFFRACTION (1.8 Å)
Cite:Role of proline residues in human lysozyme stability: a scanning calorimetric study combined with X-ray structure analysis of proline mutants.
Biochemistry, 31, 1992
1GB7
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BU of 1gb7 by Molmil
CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS
Descriptor: LYSOZYME, SODIUM ION
Authors:Funahashi, J, Takano, K, Yamagata, Y, Yutani, K.
Deposit date:2000-06-26
Release date:2000-07-27
Last modified:2023-12-27
Method:X-RAY DIFFRACTION (1.8 Å)
Cite:Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions.
Biochemistry, 39, 2000
1GBX
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BU of 1gbx by Molmil
CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS
Descriptor: LYSOZYME, SODIUM ION
Authors:Funahashi, J, Takano, K, Yamagata, Y, Yutani, K.
Deposit date:2000-06-26
Release date:2000-07-27
Last modified:2023-12-27
Method:X-RAY DIFFRACTION (1.8 Å)
Cite:Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions.
Biochemistry, 39, 2000
1GB2
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CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS
Descriptor: LYSOZYME, SODIUM ION
Authors:Funahashi, J, Takano, K, Yamagata, Y, Yutani, K.
Deposit date:2000-06-26
Release date:2000-07-27
Last modified:2023-12-27
Method:X-RAY DIFFRACTION (1.8 Å)
Cite:Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions.
Biochemistry, 39, 2000
1GB9
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BU of 1gb9 by Molmil
CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS
Descriptor: LYSOZYME, SODIUM ION
Authors:Funahashi, J, Takano, K, Yamagata, Y, Yutani, K.
Deposit date:2000-06-26
Release date:2000-07-27
Last modified:2023-12-27
Method:X-RAY DIFFRACTION (1.8 Å)
Cite:Role of surface hydrophobic residues in the conformational stability of human lysozyme at three different positions.
Biochemistry, 39, 2000
1GF8
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BU of 1gf8 by Molmil
CRYSTAL STRUCTURE OF MUTANT HUMAN LYSOZYME SUBSTITUTED AT THE SURFACE POSITIONS
Descriptor: LYSOZYME, SODIUM ION
Authors:Funahashi, J, Takano, K, Yamagata, Y, Yutani, K.
Deposit date:2000-12-04
Release date:2000-12-20
Last modified:2023-12-27
Method:X-RAY DIFFRACTION (1.8 Å)
Cite:Positive contribution of hydration structure on the surface of human lysozyme to the conformational stability.
J.Biol.Chem., 277, 2002
1GAZ
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Crystal Structure of Mutant Human Lysozyme Substituted at the Surface Positions
Descriptor: LYSOZYME, SODIUM ION
Authors:Funahashi, J, Takano, K, Yamagata, Y, Yutani, K.
Deposit date:2000-06-26
Release date:2000-07-27
Last modified:2023-12-27
Method:X-RAY DIFFRACTION (1.8 Å)
Cite:Role of amino acid residues at turns in the conformational stability and folding of human lysozyme.
Biochemistry, 39, 2000

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