1bl3
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1bl3 |SIZE=350|CAPTION= <scene name='initialview01'>1bl3</scene>, resolution 2.00Å | |PDB= 1bl3 |SIZE=350|CAPTION= <scene name='initialview01'>1bl3</scene>, resolution 2.00Å | ||
|SITE= <scene name='pdbsite=ACT:Active+Site.+Mg-Binding+Site'>ACT</scene> | |SITE= <scene name='pdbsite=ACT:Active+Site.+Mg-Binding+Site'>ACT</scene> | ||
| - | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM ION'>MG</scene> | + | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bl3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bl3 OCA], [http://www.ebi.ac.uk/pdbsum/1bl3 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1bl3 RCSB]</span> | ||
}} | }} | ||
| Line 27: | Line 30: | ||
[[Category: Mikol, V.]] | [[Category: Mikol, V.]] | ||
[[Category: Zhou-Liu, Q.]] | [[Category: Zhou-Liu, Q.]] | ||
| - | [[Category: MG]] | ||
[[Category: aid]] | [[Category: aid]] | ||
[[Category: dna binding (viral)]] | [[Category: dna binding (viral)]] | ||
| Line 36: | Line 38: | ||
[[Category: polyprotein]] | [[Category: polyprotein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:03:11 2008'' |
Revision as of 16:03, 30 March 2008
| |||||||
| , resolution 2.00Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CATALYTIC DOMAIN OF HIV-1 INTEGRASE
Overview
Human immunodeficiency virus (HIV) integrase is the enzyme responsible for insertion of a DNA copy of the viral genome into host DNA, an essential step in the replication cycle of HIV. HIV-1 integrase comprises three functional and structural domains: an N-terminal zinc-binding domain, a catalytic core domain and a C-terminal DNA-binding domain. The catalytic core domain with the F185H mutation has been crystallized without sodium cacodylate in a new crystal form, free and complexed with the catalytic metal Mg2+. The structures have been determined and refined to about 2.2 A. Unlike the previously reported structures, the three active-site carboxylate residues (D,D-35-E motif) are well ordered and both aspartate residues delineate a proper metal-binding site. Comparison of the active binding site of this domain with that of other members from the polynucleotidyl transferases superfamily shows a high level of similarity, providing a confident template for the design of antiviral agents.
About this Structure
1BL3 is a Single protein structure of sequence from Human immunodeficiency virus 1. Full crystallographic information is available from OCA.
Reference
Crystal structures of the catalytic domain of HIV-1 integrase free and complexed with its metal cofactor: high level of similarity of the active site with other viral integrases., Maignan S, Guilloteau JP, Zhou-Liu Q, Clement-Mella C, Mikol V, J Mol Biol. 1998 Sep 18;282(2):359-68. PMID:9735293
Page seeded by OCA on Sun Mar 30 19:03:11 2008
