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| Reaction Details | |||
|---|---|---|---|
 | Report a problem with these data | ||
| Cell Reactant: | HIV-1 Protease C Subtype | ||
| Syringe Reactant: | BDBM580 | ||
| Meas. Tech.: | Isothermal Titration Calorimetry | ||
| Entry Date: | 06/22/04 | ||
| ΔG°: | -62.3± (kJ/mole) | ||
| pH: | 5±n/a | ||
| Log10Kb: | 10.9± 9.53 | ||
| Temperature: | 298.15±n/a (K) | ||
| ΔH° : | -31.4± (kJ/mole) | ||
| ΔHobs : | -31.4± (kJ/mole) | ||
| Ionic Strength: | n/a | ||
| not known | |||
| Protons Released: | n/a | ||
| ΔCp : | n/a | ||
| Stoich. Param.: | n/a | ||
| ΔS° : | 0.1038± (kJ/mole-K) | ||
| Comments: | In displacement titration, inhibitors were injected into the calorimetric cell containing the protein prebound to a weak inhibitor acetylpepstatin. | ||
| Citation |  Velazquez-Campoy, A; Vega, S; Freire, E Amplification of the effects of drug resistance mutations by background polymorphisms in HIV-1 protease from African subtypes. Biochemistry41:8613-9 (2002) [PubMed] Article | ||
| More Info.: | Get all data from this article , ITC RUN data , Solution Info , Instrument Info | ||
| HIV-1 Protease C Subtype | |||
| Source: | Plasmid-encoded HIV-1 protease was expressed in E. coli cells. | ||
| Purity: | 99% | ||
| Prep. Method: | HIV-1 protease was purified and refolded from E. coli inclusion bodies. | ||
| Name: | HIV-1 Protease C Subtype | ||
| Synonyms: | n/a | ||
| Type: | Protein Complex | ||
| Mol. Mass.: | n/a | ||
| Description: | n/a | ||
| Components: | This complex has 2 components. | ||
| Component 1 | |||
| Name: | HIV-1 Protease C Subtype chain A | ||
| Synonyms: | HIV-1 Protease C Subtype chain B | HIV-1 Protease Mutant (Q7K/M36I/S37N/R41K/H69K/L89M) | ||
| Type: | Enzyme Subunit | ||
| Mol. Mass.: | 10772.76 | ||
| Organism: | Human immunodeficiency virus type 1 | ||
| Description: | n/a | ||
| Residue: | 99 | ||
| Sequence: |
| ||
| Component 2 | |||
| Name: | HIV-1 Protease C Subtype chain A | ||
| Synonyms: | HIV-1 Protease C Subtype chain B | HIV-1 Protease Mutant (Q7K/M36I/S37N/R41K/H69K/L89M) | ||
| Type: | Enzyme Subunit | ||
| Mol. Mass.: | 10772.76 | ||
| Organism: | Human immunodeficiency virus type 1 | ||
| Description: | n/a | ||
| Residue: | 99 | ||
| Sequence: |
| ||
| BDBM580 | |||
| Source: | From Dr. Kiso, Department of Medicinal Chemistry, Kyoto Pharmaceutical University, Kyoto, Japan). | ||
| Purity: | n/a | ||
| Prep. Method: | were used without further purification | ||
| Name | BDBM580 | ||
| Synonyms: | (4R)-3-[(2S,3S)-2-hydroxy-3-[(3-hydroxy-2-methylphenyl)formamido]-4-phenylbutanoyl]-5,5-dimethyl-N-[(2-methylphenyl)methyl]-1,3-thiazolidine-4-carboxamide | AG1776 | BDBM50288366 | JE-2147 | KNI-764 | ||
| Type | Small organic molecule | ||
| Emp. Form. | C32H37N3O5S | ||
| Mol. Mass. | 575.718 | ||
| SMILES | Cc1ccccc1CNC(=O)[C@H]1N(CSC1(C)C)C(=O)[C@@H](O)[C@H](Cc1ccccc1)NC(=O)c1cccc(O)c1C |r| | ||
| Structure | 
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