8FNQ
Structure of E138K/G140A/Q148K HIV-1 intasome with 4d bound
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 |
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 |
I | 0003676 | molecular_function | nucleic acid binding |
I | 0008270 | molecular_function | zinc ion binding |
I | 0015074 | biological_process | DNA integration |
J | 0003676 | molecular_function | nucleic acid binding |
J | 0008270 | molecular_function | zinc ion binding |
J | 0015074 | biological_process | DNA integration |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 8 |
Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:18669648 |
Chain | Residue | Details |
A | THR-46 | |
B | THR-46 | |
C | THR-46 | |
D | THR-46 | |
G | THR-46 | |
H | THR-46 | |
I | THR-46 | |
J | THR-46 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:21406692 |
Chain | Residue | Details |
A | SER-44 | |
B | SER-44 | |
C | SER-44 | |
D | SER-44 | |
G | SER-44 | |
H | SER-44 | |
I | SER-44 | |
J | SER-44 |
site_id | SWS_FT_FI3 |
Number of Residues | 16 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
A | SER-37 | |
G | SER-36 | |
H | SER-37 | |
H | SER-36 | |
I | SER-37 | |
I | SER-36 | |
J | SER-37 | |
J | SER-36 | |
A | SER-36 | |
B | SER-37 | |
B | SER-36 | |
C | SER-37 | |
C | SER-36 | |
D | SER-37 | |
D | SER-36 | |
G | SER-37 |
site_id | SWS_FT_FI4 |
Number of Residues | 8 |
Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
A | THR-29 | |
B | THR-29 | |
C | THR-29 | |
D | THR-29 | |
G | THR-29 | |
H | THR-29 | |
I | THR-29 | |
J | THR-29 |
site_id | SWS_FT_FI5 |
Number of Residues | 8 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | SER-24 | |
B | SER-24 | |
C | SER-24 | |
D | SER-24 | |
G | SER-24 | |
H | SER-24 | |
I | SER-24 | |
J | SER-24 |
site_id | SWS_FT_FI6 |
Number of Residues | 16 |
Details | MOD_RES: Omega-N-methylarginine => ECO:0000250|UniProtKB:Q61033 |
Chain | Residue | Details |
A | GLN-17 | |
G | ARG-15 | |
H | GLN-17 | |
H | ARG-15 | |
I | GLN-17 | |
I | ARG-15 | |
J | GLN-17 | |
J | ARG-15 | |
A | ARG-15 | |
B | GLN-17 | |
B | ARG-15 | |
C | GLN-17 | |
C | ARG-15 | |
D | GLN-17 | |
D | ARG-15 | |
G | GLN-17 |
site_id | SWS_FT_FI7 |
Number of Residues | 328 |
Details | ZN_FING: Integrase-type => ECO:0000255|PROSITE-ProRule:PRU00450 |
Chain | Residue | Details |
A | ASP3-GLN44 | |
B | ASP3-GLN44 | |
C | ASP3-GLN44 | |
D | ASP3-GLN44 | |
G | ASP3-GLN44 | |
H | ASP3-GLN44 | |
I | ASP3-GLN44 | |
J | ASP3-GLN44 |
site_id | SWS_FT_FI8 |
Number of Residues | 376 |
Details | DNA_BIND: Integrase-type => ECO:0000255|PROSITE-ProRule:PRU00506 |
Chain | Residue | Details |
A | PHE223-ASP270 | |
B | PHE223-ASP270 | |
C | PHE223-ASP270 | |
D | PHE223-ASP270 | |
G | PHE223-ASP270 | |
H | PHE223-ASP270 | |
I | PHE223-ASP270 | |
J | PHE223-ASP270 |
site_id | SWS_FT_FI9 |
Number of Residues | 32 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00450 |
Chain | Residue | Details |
A | HIS12 | |
C | HIS16 | |
C | CYS40 | |
C | CYS43 | |
D | HIS12 | |
D | HIS16 | |
D | CYS40 | |
D | CYS43 | |
G | HIS12 | |
G | HIS16 | |
G | CYS40 | |
A | HIS16 | |
G | CYS43 | |
H | HIS12 | |
H | HIS16 | |
H | CYS40 | |
H | CYS43 | |
I | HIS12 | |
I | HIS16 | |
I | CYS40 | |
I | CYS43 | |
J | HIS12 | |
A | CYS40 | |
J | HIS16 | |
J | CYS40 | |
J | CYS43 | |
A | CYS43 | |
B | HIS12 | |
B | HIS16 | |
B | CYS40 | |
B | CYS43 | |
C | HIS12 |
site_id | SWS_FT_FI10 |
Number of Residues | 16 |
Details | BINDING: |
Chain | Residue | Details |
A | ASP64 | |
G | ASP116 | |
H | ASP64 | |
H | ASP116 | |
I | ASP64 | |
I | ASP116 | |
J | ASP64 | |
J | ASP116 | |
A | ASP116 | |
B | ASP64 | |
B | ASP116 | |
C | ASP64 | |
C | ASP116 | |
D | ASP64 | |
D | ASP116 | |
G | ASP64 |
site_id | SWS_FT_FI11 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P04585 |
Chain | Residue | Details |
A | GLU152 | |
B | GLU152 | |
C | GLU152 | |
D | GLU152 | |
G | GLU152 | |
H | GLU152 | |
I | GLU152 | |
J | GLU152 |