7Z2B
P. berghei kinesin-8B motor domain in AMPPNP state bound to tubulin dimer
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000226 | biological_process | microtubule cytoskeleton organization |
A | 0000278 | biological_process | mitotic cell cycle |
A | 0003924 | molecular_function | GTPase activity |
A | 0005200 | molecular_function | structural constituent of cytoskeleton |
A | 0005525 | molecular_function | GTP binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005856 | cellular_component | cytoskeleton |
A | 0005874 | cellular_component | microtubule |
A | 0007017 | biological_process | microtubule-based process |
A | 0015630 | cellular_component | microtubule cytoskeleton |
A | 0016787 | molecular_function | hydrolase activity |
A | 0046872 | molecular_function | metal ion binding |
H | 0000226 | biological_process | microtubule cytoskeleton organization |
H | 0000278 | biological_process | mitotic cell cycle |
H | 0003924 | molecular_function | GTPase activity |
H | 0005200 | molecular_function | structural constituent of cytoskeleton |
H | 0005515 | molecular_function | protein binding |
H | 0005525 | molecular_function | GTP binding |
H | 0005737 | cellular_component | cytoplasm |
H | 0005856 | cellular_component | cytoskeleton |
H | 0005874 | cellular_component | microtubule |
H | 0007017 | biological_process | microtubule-based process |
H | 0046872 | molecular_function | metal ion binding |
K | 0003777 | molecular_function | microtubule motor activity |
K | 0005524 | molecular_function | ATP binding |
K | 0007018 | biological_process | microtubule-based movement |
K | 0008017 | molecular_function | microtubule binding |
Functional Information from PROSITE/UniProt
site_id | PS00227 |
Number of Residues | 7 |
Details | TUBULIN Tubulin subunits alpha, beta, and gamma signature. GGGTGSG |
Chain | Residue | Details |
A | GLY142-GLY148 | |
H | GLY142-GLY148 |
site_id | PS00228 |
Number of Residues | 4 |
Details | TUBULIN_B_AUTOREG Tubulin-beta mRNA autoregulation signal. MREI |
Chain | Residue | Details |
H | MET1-ILE4 |
site_id | PS00411 |
Number of Residues | 12 |
Details | KINESIN_MOTOR_1 Kinesin motor domain signature. GKLcVIDLAGSE |
Chain | Residue | Details |
K | GLY238-GLU249 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 7 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q13509 |
Chain | Residue | Details |
H | GLN11 | |
H | SER140 | |
H | GLY144 | |
H | THR145 | |
H | GLY146 | |
H | ASN206 | |
H | ASN228 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P68363 |
Chain | Residue | Details |
H | GLU71 | |
A | THR80 | |
A | PHE149 | |
A | LEU153 | |
A | MET154 | |
A | ILE188 | |
A | ARG215 | |
A | SER237 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P99024 |
Chain | Residue | Details |
H | SER40 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024 |
Chain | Residue | Details |
H | LYS60 | |
A | SER241 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q13885 |
Chain | Residue | Details |
H | SER174 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P07437 |
Chain | Residue | Details |
H | THR287 | |
H | THR292 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | MOD_RES: Omega-N-methylarginine => ECO:0000250|UniProtKB:P07437 |
Chain | Residue | Details |
H | ARG320 | |
A | SER379 |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P07437 |
Chain | Residue | Details |
H | LYS60 |
site_id | SWS_FT_FI9 |
Number of Residues | 2 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P07437 |
Chain | Residue | Details |
H | LYS326 |