Structure of PDB 1msn Chain B

Receptor sequence
>1msnB (length=99) Species: 11676 (Human immunodeficiency virus 1) [Search protein sequence]
PQITLWKRPLVTIKIGGQLKEALLDTGADDTVIEEMSLPGRWKPKMIGGI
GGFIKVRQYDQIIIEICGHKAIGTVLVGPTPFNVIGRNLLTQIGCTLNF
3D structure
PDB1msn A structural and thermodynamic escape mechanism from a drug resistant mutation of the HIV-1 protease.
ChainB
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) D25 T26 G27
Catalytic site (residue number reindexed from 1) D25 T26 G27
Enzyme Commision number 2.7.7.-
2.7.7.49: RNA-directed DNA polymerase.
2.7.7.7: DNA-directed DNA polymerase.
3.1.-.-
3.1.13.2: exoribonuclease H.
3.1.26.13: retroviral ribonuclease H.
3.4.23.16: HIV-1 retropepsin.
Interaction with ligand
Site
#
Ligand Ligand
chain
Binding residues on receptor
(original residue number in PDB)
Binding residues on receptor
(residue number reindexed from 1)
Binding affinity
BS01 JE2 B D25 G27 A28 D29 D30 I50 F82 D25 G27 A28 D29 D30 I50 F82 MOAD: Kd<1nM
PDBbind-CN: -logKd/Ki=9.09,Kd=0.81nM
Gene Ontology
Molecular Function
GO:0004190 aspartic-type endopeptidase activity
Biological Process
GO:0006508 proteolysis

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:1msn, PDBe:1msn, PDBj:1msn
PDBsum1msn
PubMed15103623
UniProtP03367|POL_HV1BR Gag-Pol polyprotein (Gene Name=gag-pol)

[Back to BioLiP]