3L43
Crystal structure of the dynamin 3 GTPase domain bound with GDP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003924 | molecular_function | GTPase activity |
| A | 0005525 | molecular_function | GTP binding |
| B | 0003924 | molecular_function | GTPase activity |
| B | 0005525 | molecular_function | GTP binding |
| C | 0003924 | molecular_function | GTPase activity |
| C | 0005525 | molecular_function | GTP binding |
| D | 0003924 | molecular_function | GTPase activity |
| D | 0005525 | molecular_function | GTP binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE GDP A 901 |
| Chain | Residue |
| A | SER41 |
| A | LEU209 |
| A | ASN236 |
| A | ARG237 |
| A | SER238 |
| A | GLN239 |
| A | ILE242 |
| A | HOH1003 |
| D | ASP211 |
| A | ALA42 |
| A | GLY43 |
| A | LYS44 |
| A | SER45 |
| A | SER46 |
| A | ARG59 |
| A | LYS206 |
| A | ASP208 |
| site_id | AC2 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE GDP B 901 |
| Chain | Residue |
| B | SER41 |
| B | ALA42 |
| B | GLY43 |
| B | LYS44 |
| B | SER45 |
| B | SER46 |
| B | ARG59 |
| B | LYS206 |
| B | ASP208 |
| B | LEU209 |
| B | VAL235 |
| B | ASN236 |
| B | ARG237 |
| B | SER238 |
| B | GLN239 |
| B | ILE242 |
| B | HOH1005 |
| B | HOH1011 |
| C | ASP211 |
| site_id | AC3 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE GDP C 901 |
| Chain | Residue |
| B | ASP211 |
| C | SER41 |
| C | ALA42 |
| C | GLY43 |
| C | LYS44 |
| C | SER45 |
| C | SER46 |
| C | ARG59 |
| C | LYS206 |
| C | ASP208 |
| C | LEU209 |
| C | ASN236 |
| C | ARG237 |
| C | SER238 |
| C | GLN239 |
| C | ILE242 |
| site_id | AC4 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE GDP D 901 |
| Chain | Residue |
| A | ASP211 |
| D | SER41 |
| D | ALA42 |
| D | GLY43 |
| D | LYS44 |
| D | SER45 |
| D | SER46 |
| D | ARG59 |
| D | LYS206 |
| D | ASP208 |
| D | LEU209 |
| D | ASN236 |
| D | ARG237 |
| D | SER238 |
| D | GLN239 |
| D | ILE242 |
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 |
| A | LEU57-ARG66 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 28 |
| Details | Region: {"description":"G1 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01055","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Region: {"description":"G2 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01055","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | Region: {"description":"G3 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01055","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | Region: {"description":"G4 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01055","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 12 |
| Details | Region: {"description":"G5 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01055","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 68 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"DEC-2009","submissionDatabase":"PDB data bank","title":"Crystal structure of the dynamin 3 GTPase domain bound with GDP.","authoringGroup":["Structural genomics consortium (SGC)"]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P39052","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |






