2X7A
Structural basis of HIV-1 tethering to membranes by the Bst2-tetherin ectodomain
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0051607 | biological_process | defense response to virus |
B | 0051607 | biological_process | defense response to virus |
C | 0051607 | biological_process | defense response to virus |
D | 0051607 | biological_process | defense response to virus |
E | 0051607 | biological_process | defense response to virus |
F | 0051607 | biological_process | defense response to virus |
G | 0051607 | biological_process | defense response to virus |
H | 0051607 | biological_process | defense response to virus |
I | 0051607 | biological_process | defense response to virus |
J | 0051607 | biological_process | defense response to virus |
K | 0051607 | biological_process | defense response to virus |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE NA B 1148 |
Chain | Residue |
B | LYS106 |
B | CL1149 |
G | THR90 |
site_id | AC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL B 1149 |
Chain | Residue |
B | LEU102 |
B | NA1148 |
site_id | AC3 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL E 1147 |
Chain | Residue |
F | NA1148 |
site_id | AC4 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE NA F 1148 |
Chain | Residue |
E | CL1147 |
F | LYS106 |
site_id | AC5 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL F 1149 |
Chain | Residue |
F | ALA89 |
site_id | AC6 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE GOL G 1142 |
Chain | Residue |
G | SER101 |
G | CL1143 |
site_id | AC7 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL G 1143 |
Chain | Residue |
A | THR94 |
G | GOL1142 |
site_id | AC8 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE NA G 1145 |
Chain | Residue |
G | ASP103 |
G | CL1144 |
site_id | AC9 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL G 1144 |
Chain | Residue |
G | GLN110 |
G | NA1145 |
site_id | BC1 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE NA H 1144 |
Chain | Residue |
H | CL1145 |
site_id | BC2 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL H 1145 |
Chain | Residue |
H | NA1144 |
site_id | BC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MG I 1148 |
Chain | Residue |
I | ASN141 |
J | LEU137 |
J | ASN141 |
site_id | BC4 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE NA I 1149 |
Chain | Residue |
I | LYS106 |
site_id | BC5 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE NA J 1148 |
Chain | Residue |
J | CL1149 |
site_id | BC6 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL J 1149 |
Chain | Residue |
J | NA1148 |
K | THR94 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 11 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19737401, ECO:0000269|PubMed:19879838 |
Chain | Residue | Details |
A | ASN92 | |
J | ASN92 | |
K | ASN92 | |
B | ASN92 | |
C | ASN92 | |
D | ASN92 | |
E | ASN92 | |
F | ASN92 | |
G | ASN92 | |
H | ASN92 | |
I | ASN92 |