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1NH0

1.03 A structure of HIV-1 protease: inhibitor binding inside and outside the active site

Summary for 1NH0
Entry DOI10.2210/pdb1nh0/pdb
Related PRD IDPRD_000401
DescriptorPROTEASE RETROPEPSIN, peptidomimetic inhibitor KI2-PHE-GLU-GLU-NH2, SULFATE ION, ... (5 entities in total)
Functional Keywordsaspartyl protease, human immunodeficiency virus, inhibitor design, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
Biological sourceHuman immunodeficiency virus 1
Cellular locationMatrix protein p17: Virion (Potential). Capsid protein p24: Virion (Potential). Nucleocapsid protein p7: Virion (Potential). Reverse transcriptase/ribonuclease H: Virion (Potential). Integrase: Virion (Potential): P03367
Total number of polymer chains4
Total formula weight23421.42
Authors
Brynda, J.,Rezacova, P.,Fabry, M.,Horejsi, M.,Hradilek, M.,Soucek, M.,Konvalinka, J.,Sedlacek, J. (deposition date: 2002-12-18, release date: 2004-04-13, Last modification date: 2023-08-16)
Primary citationBrynda, J.,Rezacova, P.,Fabry, M.,Horejsi, M.,Stouracova, R.,Sedlacek, J.,Soucek, M.,Hradilek, M.,Lepsik, M.,Konvalinka, J.
A Phenylnorstatine Inhibitor Binding to HIV-1 Protease: Geometry, Protonation, and Subsite-Pocket Interactions Analyzed at Atomic Resolution
J.Med.Chem., 47:2030-2036, 2004
Cited by
PubMed: 15056001
DOI: 10.1021/jm031105q
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.03 Å)
Structure validation

221051

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