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PDB: 9 件
1LAM
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LEUCINE AMINOPEPTIDASE (UNLIGATED)
分子名称: (4R)-2-METHYLPENTANE-2,4-DIOL, CARBONATE ION, LEUCINE AMINOPEPTIDASE, ...
著者Straeter, N, Lipscomb, W.N.
登録日1995-08-11
公開日1995-10-15
最終更新日2024-02-14
実験手法X-RAY DIFFRACTION (1.6 Å)
主引用文献Two-metal ion mechanism of bovine lens leucine aminopeptidase: active site solvent structure and binding mode of L-leucinal, a gem-diolate transition state analogue, by X-ray crystallography.
Biochemistry, 34, 1995
1LCP
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BU of 1lcp by Molmil
BOVINE LENS LEUCINE AMINOPEPTIDASE COMPLEXED WITH L-LEUCINE PHOSPHONIC ACID
分子名称: (4R)-2-METHYLPENTANE-2,4-DIOL, LEUCINE AMINOPEPTIDASE, LEUCINE PHOSPHONIC ACID, ...
著者Straeter, N, Lipscomb, W.N.
登録日1995-05-12
公開日1995-07-31
最終更新日2024-02-14
実験手法X-RAY DIFFRACTION (1.65 Å)
主引用文献Transition state analogue L-leucinephosphonic acid bound to bovine lens leucine aminopeptidase: X-ray structure at 1.65 A resolution in a new crystal form.
Biochemistry, 34, 1995
2J9A
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blLAP in Complex with Microginin FR1
分子名称: (2S,3R)-3-AMINO-2-HYDROXYDECANOIC ACID, (4S)-2-METHYL-2,4-PENTANEDIOL, CHLORIDE ION, ...
著者Kraft, M, Schleberger, C, Weckesser, J, Schulz, G.E.
登録日2006-11-06
公開日2006-12-06
最終更新日2023-12-13
実験手法X-RAY DIFFRACTION (1.73 Å)
主引用文献Binding Structure of the Leucine Aminopeptidase Inhibitor Microginin Fr1.
FEBS Lett., 580, 2006
2EWB
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The crystal structure of Bovine Lens Leucine Aminopeptidase in complex with zofenoprilat
分子名称: (4S)-2-METHYL-2,4-PENTANEDIOL, CARBONATE ION, Cytosol aminopeptidase, ...
著者Alterio, V, Pedone, C, De Simone, G.
登録日2005-11-02
公開日2006-04-04
最終更新日2023-08-23
実験手法X-RAY DIFFRACTION (1.85 Å)
主引用文献Metal Ion Substitution in the Catalytic Site Greatly Affects the Binding of Sulfhydryl-Containing Compounds to Leucyl Aminopeptidase.
Biochemistry, 45, 2006
1LAN
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BU of 1lan by Molmil
LEUCINE AMINOPEPTIDASE COMPLEX WITH L-LEUCINAL
分子名称: (4R)-2-METHYLPENTANE-2,4-DIOL, LEUCINE, LEUCINE AMINOPEPTIDASE, ...
著者Straeter, N, Lipscomb, W.N.
登録日1995-08-11
公開日1995-10-15
最終更新日2024-02-14
実験手法X-RAY DIFFRACTION (1.9 Å)
主引用文献Two-metal ion mechanism of bovine lens leucine aminopeptidase: active site solvent structure and binding mode of L-leucinal, a gem-diolate transition state analogue, by X-ray crystallography.
Biochemistry, 34, 1995
1BLL
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BU of 1bll by Molmil
X-RAY CRYSTALLOGRAPHIC DETERMINATION OF THE STRUCTURE OF BOVINE LENS LEUCINE AMINOPEPTIDASE COMPLEXED WITH AMASTATIN: FORMULATION OF A CATALYTIC MECHANISM FEATURING A GEM-DIOLATE TRANSITION STATE
分子名称: AMASTATIN, LEUCINE AMINOPEPTIDASE, ZINC ION
著者Kim, H, Lipscomb, W.N.
登録日1993-03-02
公開日1994-01-31
最終更新日2023-11-15
実験手法X-RAY DIFFRACTION (2.4 Å)
主引用文献X-ray crystallographic determination of the structure of bovine lens leucine aminopeptidase complexed with amastatin: formulation of a catalytic mechanism featuring a gem-diolate transition state.
Biochemistry, 32, 1993
1LAP
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MOLECULAR STRUCTURE OF LEUCINE AMINOPEPTIDASE AT 2.7-ANGSTROMS RESOLUTION
分子名称: Cytosol aminopeptidase, ZINC ION
著者Burley, S.K, David, P.R, Taylor, A, Lipscomb, W.N.
登録日1990-08-01
公開日1991-10-15
最終更新日2024-02-14
実験手法X-RAY DIFFRACTION (2.7 Å)
主引用文献Molecular structure of leucine aminopeptidase at 2.7-A resolution.
Proc.Natl.Acad.Sci.USA, 87, 1990
1BPN
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DIFFERENTIATION AND IDENTIFICATION OF THE TWO CATALYTIC METAL BINDING SITES IN BOVINE LENS LEUCINE AMINOPEPTIDASE BY X-RAY CRYSTALLOGRAPHY
分子名称: LEUCINE AMINOPEPTIDASE, ZINC ION
著者Kim, H, Lipscomb, W.N.
登録日1993-03-02
公開日1993-07-15
最終更新日2024-02-07
実験手法X-RAY DIFFRACTION (2.9 Å)
主引用文献Differentiation and identification of the two catalytic metal binding sites in bovine lens leucine aminopeptidase by x-ray crystallography.
Proc.Natl.Acad.Sci.USA, 90, 1993
1BPM
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BU of 1bpm by Molmil
DIFFERENTIATION AND IDENTIFICATION OF THE TWO CATALYTIC METAL BINDING SITES IN BOVINE LENS LEUCINE AMINOPEPTIDASE BY X-RAY CRYSTALLOGRAPHY
分子名称: LEUCINE AMINOPEPTIDASE, MAGNESIUM ION, ZINC ION
著者Kim, H, Lipscomb, W.N.
登録日1993-03-02
公開日1993-07-15
最終更新日2024-02-07
実験手法X-RAY DIFFRACTION (2.9 Å)
主引用文献Differentiation and identification of the two catalytic metal binding sites in bovine lens leucine aminopeptidase by x-ray crystallography.
Proc.Natl.Acad.Sci.USA, 90, 1993

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