7KU7
Cryo-EM structure of Rous sarcoma virus cleaved synaptic complex (CSC) with HIV-1 integrase strand transfer inhibitor MK-2048. Cluster identified by 3-dimensional variability analysis in cryoSPARC.
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003676 | molecular_function | nucleic acid binding |
A | 0008270 | molecular_function | zinc ion binding |
A | 0015074 | biological_process | DNA integration |
B | 0003676 | molecular_function | nucleic acid binding |
B | 0008270 | molecular_function | zinc ion binding |
B | 0015074 | biological_process | DNA integration |
C | 0003676 | molecular_function | nucleic acid binding |
C | 0008270 | molecular_function | zinc ion binding |
C | 0015074 | biological_process | DNA integration |
D | 0003676 | molecular_function | nucleic acid binding |
D | 0008270 | molecular_function | zinc ion binding |
D | 0015074 | biological_process | DNA integration |
E | 0003676 | molecular_function | nucleic acid binding |
E | 0008270 | molecular_function | zinc ion binding |
E | 0015074 | biological_process | DNA integration |
F | 0003676 | molecular_function | nucleic acid binding |
F | 0008270 | molecular_function | zinc ion binding |
F | 0015074 | biological_process | DNA integration |
G | 0003676 | molecular_function | nucleic acid binding |
G | 0008270 | molecular_function | zinc ion binding |
G | 0015074 | biological_process | DNA integration |
H | 0003676 | molecular_function | nucleic acid binding |
H | 0008270 | molecular_function | zinc ion binding |
H | 0015074 | biological_process | DNA integration |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 384 |
Details | DNA_BIND: Integrase-type => ECO:0000255|PROSITE-ProRule:PRU00506 |
Chain | Residue | Details |
A | PRO222-THR270 | |
B | PRO222-THR270 | |
C | PRO222-THR270 | |
D | PRO222-THR270 | |
E | PRO222-THR270 | |
F | PRO222-THR270 | |
G | PRO222-THR270 | |
H | PRO222-THR270 |
site_id | SWS_FT_FI2 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00450 |
Chain | Residue | Details |
A | HIS9 | |
E | HIS13 | |
F | HIS9 | |
F | HIS13 | |
G | HIS9 | |
G | HIS13 | |
H | HIS9 | |
H | HIS13 | |
A | HIS13 | |
B | HIS9 | |
B | HIS13 | |
C | HIS9 | |
C | HIS13 | |
D | HIS9 | |
D | HIS13 | |
E | HIS9 |
site_id | SWS_FT_FI3 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00450, ECO:0000269|PubMed:26887497 |
Chain | Residue | Details |
A | CYS37 | |
E | CYS40 | |
F | CYS37 | |
F | CYS40 | |
G | CYS37 | |
G | CYS40 | |
H | CYS37 | |
H | CYS40 | |
A | CYS40 | |
B | CYS37 | |
B | CYS40 | |
C | CYS37 | |
C | CYS40 | |
D | CYS37 | |
D | CYS40 | |
E | CYS37 |
site_id | SWS_FT_FI4 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00405, ECO:0000269|PubMed:10669607 |
Chain | Residue | Details |
A | ASP64 | |
E | ASP121 | |
F | ASP64 | |
F | ASP121 | |
G | ASP64 | |
G | ASP121 | |
H | ASP64 | |
H | ASP121 | |
A | ASP121 | |
B | ASP64 | |
B | ASP121 | |
C | ASP64 | |
C | ASP121 | |
D | ASP64 | |
D | ASP121 | |
E | ASP64 |
site_id | SWS_FT_FI5 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10669607 |
Chain | Residue | Details |
A | GLU157 | |
B | GLU157 | |
C | GLU157 | |
D | GLU157 | |
E | GLU157 | |
F | GLU157 | |
G | GLU157 | |
H | GLU157 |