4KVA
GTPase domain of Septin 10 from Schistosoma mansoni in complex with GTP
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0003924 | molecular_function | GTPase activity |
A | 0005525 | molecular_function | GTP binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005856 | cellular_component | cytoskeleton |
A | 0019003 | molecular_function | GDP binding |
A | 0031105 | cellular_component | septin complex |
A | 0031982 | cellular_component | vesicle |
A | 0042802 | molecular_function | identical protein binding |
A | 0042803 | molecular_function | protein homodimerization activity |
A | 0046872 | molecular_function | metal ion binding |
A | 0046982 | molecular_function | protein heterodimerization activity |
A | 0051260 | biological_process | protein homooligomerization |
B | 0000287 | molecular_function | magnesium ion binding |
B | 0003924 | molecular_function | GTPase activity |
B | 0005525 | molecular_function | GTP binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005856 | cellular_component | cytoskeleton |
B | 0019003 | molecular_function | GDP binding |
B | 0031105 | cellular_component | septin complex |
B | 0031982 | cellular_component | vesicle |
B | 0042802 | molecular_function | identical protein binding |
B | 0042803 | molecular_function | protein homodimerization activity |
B | 0046872 | molecular_function | metal ion binding |
B | 0046982 | molecular_function | protein heterodimerization activity |
B | 0051260 | biological_process | protein homooligomerization |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE GTP A 500 |
Chain | Residue |
A | THR50 |
A | ASP186 |
A | VAL237 |
A | GLY238 |
A | ARG253 |
A | TYR255 |
A | MG501 |
A | HOH617 |
A | HOH630 |
A | HOH664 |
A | HOH672 |
A | GLY51 |
A | HOH691 |
B | THR157 |
B | THR187 |
B | GLU192 |
A | ILE52 |
A | GLY53 |
A | LYS54 |
A | SER55 |
A | THR56 |
A | GLU100 |
A | LYS184 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG A 501 |
Chain | Residue |
A | SER55 |
A | GLU100 |
A | GTP500 |
A | HOH690 |
A | HOH691 |
site_id | AC3 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE GTP B 500 |
Chain | Residue |
A | THR187 |
A | GLU192 |
B | THR50 |
B | GLY51 |
B | ILE52 |
B | GLY53 |
B | LYS54 |
B | SER55 |
B | THR56 |
B | GLU100 |
B | LYS184 |
B | ASP186 |
B | VAL237 |
B | GLY238 |
B | ARG253 |
B | TYR255 |
B | MG501 |
B | HOH610 |
B | HOH621 |
B | HOH628 |
B | HOH637 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG B 501 |
Chain | Residue |
B | SER55 |
B | GLU100 |
B | GTP500 |
B | HOH610 |
B | HOH699 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 14 |
Details | BINDING: BINDING => ECO:0000269|PubMed:24464615, ECO:0007744|PDB:4KVA |
Chain | Residue | Details |
A | GLY51 | |
B | GLU100 | |
B | LYS184 | |
B | GLU192 | |
B | GLY238 | |
B | ARG253 | |
A | SER55 | |
A | GLU100 | |
A | LYS184 | |
A | GLU192 | |
A | GLY238 | |
A | ARG253 | |
B | GLY51 | |
B | SER55 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498 |
Chain | Residue | Details |
A | ASN405 | |
B | ASN405 |