5NER
Localised reconstruction of alpha v beta 6 bound to Foot and Mouth Disease Virus O PanAsia - Pose A prime.
Functional Information from GO Data
Chain | GOid | namespace | contents |
1 | 0005198 | molecular_function | structural molecule activity |
1 | 0019028 | cellular_component | viral capsid |
1 | 0019062 | biological_process | virion attachment to host cell |
1 | 0039618 | cellular_component | T=pseudo3 icosahedral viral capsid |
1 | 0046718 | biological_process | symbiont entry into host cell |
2 | 0005198 | molecular_function | structural molecule activity |
3 | 0005198 | molecular_function | structural molecule activity |
4 | 0019030 | cellular_component | icosahedral viral capsid |
A | 0007155 | biological_process | cell adhesion |
A | 0008305 | cellular_component | integrin complex |
Functional Information from PROSITE/UniProt
site_id | PS00022 |
Number of Residues | 12 |
Details | EGF_1 EGF-like domain signature 1. CaChpGhmGPrC |
Chain | Residue | Details |
B | CYS459-CYS470 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | BINDING: in MIDAS binding site => ECO:0000269|PubMed:25383667, ECO:0007744|PDB:4UM8 |
Chain | Residue | Details |
B | ASP120 | |
A | ASP292 | |
A | ASP349 | |
A | ASP351 | |
A | ASP353 | |
A | PHE355 | |
A | ASP357 | |
A | ASP413 | |
A | ASP415 | |
A | ASN417 | |
A | TYR419 | |
A | ASN232 | |
A | ASP421 | |
A | ASP234 | |
A | ILE236 | |
A | ASP238 | |
A | ASP284 | |
A | ASN286 | |
A | ASP288 | |
A | TYR290 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: in MIDAS binding site => ECO:0000269|PubMed:25383667, ECO:0007744|PDB:4UM8, ECO:0007744|PDB:4UM9 |
Chain | Residue | Details |
B | SER122 | |
B | GLU220 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | BINDING: in MIDAS binding site => ECO:0000250|UniProtKB:P05106 |
Chain | Residue | Details |
B | SER124 | |
A | ASN266 | |
A | ASN458 | |
A | ASN524 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: in ADMIDAS binding site => ECO:0000269|PubMed:25383667, ECO:0007744|PDB:4UM8, ECO:0007744|PDB:4UM9 |
Chain | Residue | Details |
B | ASP127 | |
B | ASP128 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | BINDING: in LIMBS binding site => ECO:0000269|PubMed:25383667, ECO:0007744|PDB:4UM9 |
Chain | Residue | Details |
B | GLU159 | |
B | ASN215 | |
B | ASP217 | |
B | PRO219 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | BINDING: in ADMIDAS binding site and liganded-open conformation => ECO:0000250|UniProtKB:P05106 |
Chain | Residue | Details |
B | ASP251 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | BINDING: in ADMIDAS binding site and unliganded-closed conformation => ECO:0000269|PubMed:25383667, ECO:0007744|PDB:4UM8 |
Chain | Residue | Details |
B | LYS335 |
site_id | SWS_FT_FI8 |
Number of Residues | 3 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:25383667, ECO:0007744|PDB:4UM8, ECO:0007744|PDB:4UM9 |
Chain | Residue | Details |
B | ASN28 | |
B | ASN77 | |
B | ASN367 |
site_id | SWS_FT_FI9 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:25383667, ECO:0000269|PubMed:28117447, ECO:0007744|PDB:4UM8, ECO:0007744|PDB:4UM9 |
Chain | Residue | Details |
B | ASN240 |
site_id | SWS_FT_FI10 |
Number of Residues | 3 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
B | ASN376 | |
B | ASN443 | |
B | ASN451 |