(Q27643142)

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Cofactor hydrogen bonding onto the protein main chain is conserved in the short chain dehydrogenase/reductase family and contributes to nicotinamide orientation

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Cofactor hydrogen bonding onto the protein main chain is conserved in the short chain dehydrogenase/reductase family and contributes to nicotinamide orientation (English)

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Sheng-Xiang Lin

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Sheng-Xiang Lin

2

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author name string

Rong Shi

1

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language of work or name

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publication date

16 April 2004

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Journal of Biological Chemistry

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279

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16

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16778-85

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Short-chain dehydrogenases/reductases (SDR): the 2002 update

1 reference

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Short-chain dehydrogenases/reductases (SDR)

1 reference

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Involvement of up-regulation of 17beta-hydroxysteroid dehydrogenase type 1 in maintenance of intratumoral high estradiol levels in postmenopausal breast cancers

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Processing of X-ray diffraction data collected in oscillation mode

1 reference

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Refinement of macromolecular structures by the maximum-likelihood method

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PROCHECK: a program to check the stereochemical quality of protein structures

1 reference

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The Protein Data Bank

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Structure of human estrogenic 17 beta-hydroxysteroid dehydrogenase at 2.20 A resolution

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Structure of the ternary complex of human 17beta-hydroxysteroid dehydrogenase type 1 with 3-hydroxyestra-1,3,5,7-tetraen-17-one (equilin) and NADP+

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The structure of the negative transcriptional regulator NmrA reveals a structural superfamily which includes the short-chain dehydrogenase/reductases

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Crystal structure of human estrogenic 17 beta-hydroxysteroid dehydrogenase complexed with 17 beta-estradiol

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Crystallization and Preliminary X-ray Diffraction Analysis of the Complex of Human Placental 17β-Hydroxysteroid Dehydrogenase with NADP+

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Identifiers

10.1074/JBC.M313156200

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https://api.fatcat.wiki/v0/release/y5rodlhnzbb3vn34inlh3gfaza

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