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1BU1
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BU of 1bu1 by Molmil
SRC FAMILY KINASE HCK SH3 DOMAIN
分子名称: PROTEIN (HEMOPOIETIC CELL KINASE)
著者Arold, S, Franken, P, Dumas, C.
登録日1998-09-09
公開日1998-11-11
最終更新日2023-08-09
実験手法X-RAY DIFFRACTION (2.6 Å)
主引用文献RT loop flexibility enhances the specificity of Src family SH3 domains for HIV-1 Nef.
Biochemistry, 37, 1998
1O7C
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BU of 1o7c by Molmil
Solution structure of the human TSG-6 Link module in the presence of a hyaluronan octasaccharide
分子名称: TUMOR NECROSIS FACTOR-INDUCIBLE PROTEIN TSG-6
著者Blundell, C.D, Teriete, P, Kahmann, J.D, Pickford, A.R, Campbell, I.D, Day, A.J.
登録日2002-10-29
公開日2003-10-23
最終更新日2018-01-24
実験手法SOLUTION NMR
主引用文献The link module from ovulation- and inflammation-associated protein TSG-6 changes conformation on hyaluronan binding.
J. Biol. Chem., 278, 2003
1O7B
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BU of 1o7b by Molmil
Refined solution structure of the human TSG-6 Link module
分子名称: TUMOR NECROSIS FACTOR-INDUCIBLE PROTEIN TSG-6
著者Blundell, C.D, Teriete, P, Kahmann, J.D, Pickford, A.R, Campbell, I.D, Day, A.J.
登録日2002-10-29
公開日2003-10-23
最終更新日2018-01-24
実験手法SOLUTION NMR
主引用文献The link module from ovulation- and inflammation-associated protein TSG-6 changes conformation on hyaluronan binding.
J. Biol. Chem., 278, 2003
1RKM
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BU of 1rkm by Molmil
STRUCTURE OF OPPA
分子名称: OLIGO-PEPTIDE BINDING PROTEIN
著者Sleigh, S.H, Tame, J.R.H, Wilkinson, A.J.
登録日1997-03-25
公開日1997-07-29
最終更新日2023-08-09
実験手法X-RAY DIFFRACTION (2.4 Å)
主引用文献Peptide binding in OppA, the crystal structures of the periplasmic oligopeptide binding protein in the unliganded form and in complex with lysyllysine.
Biochemistry, 36, 1997
1AJ6
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BU of 1aj6 by Molmil
NOVOBIOCIN-RESISTANT MUTANT (R136H) OF THE N-TERMINAL 24 KDA FRAGMENT OF DNA GYRASE B COMPLEXED WITH NOVOBIOCIN AT 2.3 ANGSTROMS RESOLUTION
分子名称: GYRASE, NOVOBIOCIN
著者Weston, S.A, Tunnicliffe, A, Pauptit, R.A.
登録日1997-05-15
公開日1998-05-20
最終更新日2024-04-03
実験手法X-RAY DIFFRACTION (2.3 Å)
主引用文献The entropic penalty of ordered water accounts for weaker binding of the antibiotic novobiocin to a resistant mutant of DNA gyrase: a thermodynamic and crystallographic study.
Biochemistry, 36, 1997
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