8TYM
Cryo-EM of the GDP-bound human dynamin (full-length) polymer assembled on the membrane in the super constricted state
Functional Information from PROSITE/UniProt
| site_id | PS00410 |
| Number of Residues | 10 |
| Details | G_DYNAMIN_1 Dynamin-type guanine nucleotide-binding (G) domain signature. LPRGSGIVTR |
| Chain | Residue | Details |
| c | LEU57-ARG66 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:20428113, ECO:0000269|PubMed:26612256, ECO:0007744|PDB:5D3Q |
| Chain | Residue | Details |
| c | SER41 | |
| f | SER41 | |
| B | SER41 | |
| C | SER41 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:20428113, ECO:0000269|PubMed:26612256, ECO:0007744|PDB:2X2E, ECO:0007744|PDB:2X2F, ECO:0007744|PDB:5D3Q |
| Chain | Residue | Details |
| c | GLY43 | |
| B | SER45 | |
| B | LYS206 | |
| B | ASP208 | |
| C | GLY43 | |
| C | SER45 | |
| C | LYS206 | |
| C | ASP208 | |
| c | SER45 | |
| c | LYS206 | |
| c | ASP208 | |
| f | GLY43 | |
| f | SER45 | |
| f | LYS206 | |
| f | ASP208 | |
| B | GLY43 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 20 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:20428113, ECO:0000269|PubMed:26612256, ECO:0000269|PubMed:30069048, ECO:0007744|PDB:2X2E, ECO:0007744|PDB:2X2F, ECO:0007744|PDB:5D3Q, ECO:0007744|PDB:6DLU |
| Chain | Residue | Details |
| c | ALA44 | |
| f | GLN239 | |
| B | ALA44 | |
| B | SER46 | |
| B | ASN236 | |
| B | ARG237 | |
| B | GLN239 | |
| C | ALA44 | |
| C | SER46 | |
| C | ASN236 | |
| C | ARG237 | |
| c | SER46 | |
| C | GLN239 | |
| c | ASN236 | |
| c | ARG237 | |
| c | GLN239 | |
| f | ALA44 | |
| f | SER46 | |
| f | ASN236 | |
| f | ARG237 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:26612256, ECO:0007744|PDB:5D3Q |
| Chain | Residue | Details |
| c | ARG59 | |
| f | ARG59 | |
| B | ARG59 | |
| C | ARG59 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:20428113, ECO:0007744|PDB:2X2E, ECO:0007744|PDB:2X2F |
| Chain | Residue | Details |
| c | GLY60 | |
| f | GLY60 | |
| B | GLY60 | |
| C | GLY60 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:20428113, ECO:0000269|PubMed:26612256, ECO:0000269|PubMed:30069048, ECO:0007744|PDB:2X2E, ECO:0007744|PDB:5D3Q, ECO:0007744|PDB:6DLU |
| Chain | Residue | Details |
| c | ASP211 | |
| f | ASP211 | |
| B | ASP211 | |
| C | ASP211 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 8 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P39053 |
| Chain | Residue | Details |
| c | TYR80 | |
| c | TYR354 | |
| f | TYR80 | |
| f | TYR354 | |
| B | TYR80 | |
| B | TYR354 | |
| C | TYR80 | |
| C | TYR354 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphotyrosine; alternate => ECO:0000250|UniProtKB:P39053 |
| Chain | Residue | Details |
| c | TYR125 | |
| f | TYR125 | |
| B | TYR125 | |
| C | TYR125 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 8 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P39053 |
| Chain | Residue | Details |
| c | SER306 | |
| c | SER512 | |
| f | SER306 | |
| f | SER512 | |
| B | SER306 | |
| B | SER512 | |
| C | SER306 | |
| C | SER512 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P21575 |
| Chain | Residue | Details |
| c | SER347 | |
| f | SER347 | |
| B | SER347 | |
| C | SER347 |
