3UGX
Crystal Structure of Visual Arrestin
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0001664 | molecular_function | G protein-coupled receptor binding |
A | 0001750 | cellular_component | photoreceptor outer segment |
A | 0001917 | cellular_component | photoreceptor inner segment |
A | 0002031 | biological_process | G protein-coupled receptor internalization |
A | 0005829 | cellular_component | cytosol |
A | 0007165 | biological_process | signal transduction |
A | 0016020 | cellular_component | membrane |
A | 0042995 | cellular_component | cell projection |
B | 0001664 | molecular_function | G protein-coupled receptor binding |
B | 0001750 | cellular_component | photoreceptor outer segment |
B | 0001917 | cellular_component | photoreceptor inner segment |
B | 0002031 | biological_process | G protein-coupled receptor internalization |
B | 0005829 | cellular_component | cytosol |
B | 0007165 | biological_process | signal transduction |
B | 0016020 | cellular_component | membrane |
B | 0042995 | cellular_component | cell projection |
C | 0001664 | molecular_function | G protein-coupled receptor binding |
C | 0001750 | cellular_component | photoreceptor outer segment |
C | 0001917 | cellular_component | photoreceptor inner segment |
C | 0002031 | biological_process | G protein-coupled receptor internalization |
C | 0005829 | cellular_component | cytosol |
C | 0007165 | biological_process | signal transduction |
C | 0016020 | cellular_component | membrane |
C | 0042995 | cellular_component | cell projection |
D | 0001664 | molecular_function | G protein-coupled receptor binding |
D | 0001750 | cellular_component | photoreceptor outer segment |
D | 0001917 | cellular_component | photoreceptor inner segment |
D | 0002031 | biological_process | G protein-coupled receptor internalization |
D | 0005829 | cellular_component | cytosol |
D | 0007165 | biological_process | signal transduction |
D | 0016020 | cellular_component | membrane |
D | 0042995 | cellular_component | cell projection |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PTD A 405 |
Chain | Residue |
A | ASP19 |
A | LYS55 |
A | HIS155 |
A | MET198 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PTD A 406 |
Chain | Residue |
A | TYR58 |
A | GLN87 |
C | GLN87 |
C | PHE152 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PTD A 407 |
Chain | Residue |
A | TYR250 |
A | SER252 |
A | PTD412 |
A | VAL248 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PTD A 408 |
Chain | Residue |
A | THR258 |
A | ALA261 |
A | ASN286 |
A | ASN287 |
A | HOH430 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE PTD A 409 |
Chain | Residue |
A | LYS14 |
A | TYR25 |
A | PHE377 |
site_id | AC6 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE PTD A 410 |
Chain | Residue |
A | PRO127 |
A | CYS128 |
A | VAL130 |
A | GLN178 |
A | SER308 |
A | SER309 |
A | THR310 |
A | ILE311 |
A | ILE323 |
A | HOH436 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PTD A 411 |
Chain | Residue |
A | TYR125 |
C | VAL94 |
C | GLY95 |
C | ALA96 |
site_id | AC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE PTD A 412 |
Chain | Residue |
A | LYS318 |
A | LEU324 |
A | PTD407 |
site_id | AC9 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE NA A 413 |
Chain | Residue |
A | SER199 |
A | GLU231 |
site_id | BC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 414 |
Chain | Residue |
A | TYR84 |
A | PHE85 |
C | VAL88 |
C | GLN89 |
C | VAL94 |
site_id | BC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO A 415 |
Chain | Residue |
A | LYS267 |
B | PHE197 |
B | ASP200 |
site_id | BC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE IMD B 405 |
Chain | Residue |
B | ARG66 |
B | GLU70 |
B | MET131 |
B | CYS143 |
B | ASP146 |
B | HOH435 |
site_id | BC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE PTD B 406 |
Chain | Residue |
B | TYR67 |
B | TYR250 |
B | SER251 |
site_id | BC5 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE PTD B 407 |
Chain | Residue |
B | LYS318 |
B | LEU324 |
site_id | BC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NA B 408 |
Chain | Residue |
A | VAL159 |
B | GLN195 |
B | HOH411 |
B | HOH426 |
B | HOH431 |
site_id | BC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO B 409 |
Chain | Residue |
A | ASN271 |
A | SER272 |
A | SER273 |
B | GLU350 |
site_id | BC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE PTD C 405 |
Chain | Residue |
C | TYR250 |
C | SER251 |
C | SER252 |
site_id | BC9 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE PTD C 406 |
Chain | Residue |
B | ASP73 |
B | VAL74 |
B | GLY76 |
C | GLN187 |
C | PRO188 |
C | ARG189 |
C | GLU350 |
C | PRO352 |
C | HOH455 |
site_id | CC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE PTD C 407 |
Chain | Residue |
C | GLU212 |
C | THR310 |
C | VAL325 |
C | SER326 |
C | PRO352 |
C | PHE353 |
C | ARG354 |
C | HOH412 |
site_id | CC2 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE K C 408 |
Chain | Residue |
D | GLU350 |
site_id | CC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO C 409 |
Chain | Residue |
A | GLU160 |
A | ASP162 |
C | LYS150 |
C | ILE164 |
C | LYS166 |
site_id | CC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO C 410 |
Chain | Residue |
A | VAL88 |
A | GLN89 |
A | VAL94 |
C | TYR84 |
C | PHE85 |
site_id | CC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO C 411 |
Chain | Residue |
C | THR275 |
D | GLU346 |
D | ALA348 |
C | LEU274 |
site_id | CC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE IMD D 405 |
Chain | Residue |
D | ARG66 |
D | CYS143 |
D | ASP146 |
D | HOH430 |
site_id | CC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE IMD D 406 |
Chain | Residue |
D | PRO127 |
D | CYS128 |
D | VAL130 |
D | THR310 |
D | ILE323 |
D | HOH432 |
D | HOH443 |
site_id | CC8 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE PTD D 407 |
Chain | Residue |
D | LYS318 |
D | LEU324 |
site_id | CC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO D 408 |
Chain | Residue |
D | GLN187 |
D | LYS211 |
D | ILE213 |
D | TYR215 |
D | GLU218 |
Functional Information from PROSITE/UniProt
site_id | PS00295 |
Number of Residues | 19 |
Details | ARRESTINS Arrestins signature. FRYGqEDiDVMGLsFrRDL |
Chain | Residue | Details |
A | PHE65-LEU83 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | MOD_RES: N-acetylmethionine; partial => ECO:0000269|PubMed:3478675 |
Chain | Residue | Details |
A | MET1 | |
B | MET1 | |
C | MET1 | |
D | MET1 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P15887 |
Chain | Residue | Details |
A | THR230 | |
B | THR230 | |
C | THR230 | |
D | THR230 |