1F9B
 
 | | MELANIN PROTEIN INTERACTION: X-RAY STRUCTURE OF THE COMPLEX OF MARE LACTOFERRIN WITH MELANIN MONOMERS | | Descriptor: | 3H-INDOLE-5,6-DIOL, BICARBONATE ION, FE (III) ION, ... | | Authors: | Kumar, S, Singh, T.P, Sharma, A.K, Singh, N, Raman, G. | | Deposit date: | 2000-07-10 | | Release date: | 2001-02-10 | | Last modified: | 2018-01-31 | | Method: | X-RAY DIFFRACTION (2.7 Å) | | Cite: | Lactoferrin-melanin interaction and its possible implications in melanin polymerization: crystal structure of the complex formed between mare lactoferrin and melanin monomers at 2.7-A resolution.
Proteins, 45, 2001
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1OYO
 | | Regulation of protease activity by melanin: Crystal structure of the complex formed between proteinase K and melanin monomers at 2.0 resolution | | Descriptor: | 3H-INDOLE-5,6-DIOL, CALCIUM ION, Proteinase K | | Authors: | Singh, N, Sharma, S, Kumar, S, Raman, G, Singh, T.P. | | Deposit date: | 2003-04-06 | | Release date: | 2003-05-20 | | Last modified: | 2024-04-03 | | Method: | X-RAY DIFFRACTION (2.02 Å) | | Cite: | Regulation of protease activity by melanin: Crystal structure of the complex formed between proteinase K and melanin monomers at 2.0 resolution
To be Published
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2KYX
 | | Solution structure of the RRM domain of CYP33 | | Descriptor: | Peptidyl-prolyl cis-trans isomerase E | | Authors: | Park, S, Bushweller, J.H. | | Deposit date: | 2010-06-09 | | Release date: | 2010-08-25 | | Last modified: | 2023-06-14 | | Method: | SOLUTION NMR | | Cite: | The PHD3 domain of MLL acts as a CYP33-regulated switch between MLL-mediated activation and repression .
Biochemistry, 49, 2010
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2KYU
 | | The solution structure of the PHD3 finger of MLL | | Descriptor: | Histone-lysine N-methyltransferase MLL, ZINC ION | | Authors: | Park, S, Bushweller, J.H. | | Deposit date: | 2010-06-08 | | Release date: | 2010-08-25 | | Last modified: | 2020-02-05 | | Method: | SOLUTION NMR | | Cite: | The PHD3 domain of MLL acts as a CYP33-regulated switch between MLL-mediated activation and repression.
Biochemistry, 49, 2010
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