Your browser does not support inline frames or is currently configured not to display inline frames. Content can be viewed at actual source page: inc/head.html
PDBsum entry 4ll3
Go to PDB code:
Hydrolase/hydrolase inhibitor
PDB id
4ll3
Loading ...
Contents
Protein chains
99 a.a.
Ligands
017-017
Waters
×141
PDB id:
4ll3
Links
PDBe
RCSB
MMDB
JenaLib
Proteopedia
CATH
SCOP
PDBSWS
PDBePISA
ProSAT
Name:
Hydrolase/hydrolase inhibitor
Title:
Structure of wild-type HIV protease in complex with darunavir
Structure:
Protease. Chain: a, b. Fragment: unp residues 7-105. Engineered: yes
Source:
Human immunodeficiency virus 1. Organism_taxid: 11676
Resolution:
1.95Å
R-factor:
0.185
R-free:
0.230
Authors:
K.Grantz Saskova,P.Rezacova,J.Brynda,M.Kozisek,J.Konvalinka
Key ref:
M.Kožíšek et al. (2014). Thermodynamic and structural analysis of HIV protease resistance to darunavir - analysis of heavily mutated patient-derived HIV-1 proteases.
Febs J
,
281
, 1834-1847.
PubMed id:
24785545
DOI:
10.1111/febs.12743
Date:
09-Jul-13
Release date:
16-Apr-14
Supersedes:
3qoz
PROCHECK
Headers
References
Protein chains
?
Q9WFL7
(Q9WFL7_9HIV1) - Pol polyprotein (Fragment) from Human immunodeficiency virus 1
Seq:
Struc:
347 a.a.
99 a.a.
Key:
PfamA domain
Secondary structure
CATH domain
Enzyme reactions
Enzyme class:
E.C.?
[IntEnz]
[ExPASy]
[KEGG]
[BRENDA]
DOI no:
10.1111/febs.12743
Febs J
281
:1834-1847 (2014)
PubMed id:
24785545
Thermodynamic and structural analysis of HIV protease resistance to darunavir - analysis of heavily mutated patient-derived HIV-1 proteases.
M.Kožíšek,
M.Lepšík,
K.Grantz Šašková,
J.Brynda,
J.Konvalinka,
P.Rezáčová.
ABSTRACT
No abstract given.
'); } }