Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003777 | molecular_function | microtubule motor activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0007018 | biological_process | microtubule-based movement |
| A | 0008017 | molecular_function | microtubule binding |
| B | 0003777 | molecular_function | microtubule motor activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0007018 | biological_process | microtubule-based movement |
| B | 0008017 | molecular_function | microtubule binding |
| C | 0003777 | molecular_function | microtubule motor activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0007018 | biological_process | microtubule-based movement |
| C | 0008017 | molecular_function | microtubule binding |
| D | 0003777 | molecular_function | microtubule motor activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0007018 | biological_process | microtubule-based movement |
| D | 0008017 | molecular_function | microtubule binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | binding site for residue MG A 601 |
| Chain | Residue |
| A | THR355 |
| A | ADP602 |
| A | HOH704 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | binding site for residue ADP A 602 |
| Chain | Residue |
| A | GLY353 |
| A | LYS354 |
| A | THR355 |
| A | HIS356 |
| A | MG601 |
| A | ARG264 |
| A | PRO267 |
| A | GLN349 |
| A | THR350 |
| A | GLY351 |
| A | SER352 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue MG A 603 |
| Chain | Residue |
| A | LEU273 |
| A | GLU277 |
| A | HOH708 |
| A | HOH714 |
| site_id | AC4 |
| Number of Residues | 13 |
| Details | binding site for residue ADP B 601 |
| Chain | Residue |
| B | ARG264 |
| B | ARG266 |
| B | PRO267 |
| B | GLN349 |
| B | THR350 |
| B | GLY351 |
| B | SER352 |
| B | GLY353 |
| B | LYS354 |
| B | THR355 |
| B | HIS356 |
| B | MG603 |
| B | HOH713 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | binding site for residue MG B 602 |
| Chain | Residue |
| B | LEU243 |
| B | HOH704 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue MG B 603 |
| Chain | Residue |
| B | THR355 |
| B | ADP601 |
| B | HOH701 |
| B | HOH717 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue MG C 601 |
| Chain | Residue |
| C | THR355 |
| C | ARG456 |
| C | SER467 |
| C | ADP602 |
| C | HOH707 |
| site_id | AC8 |
| Number of Residues | 11 |
| Details | binding site for residue ADP C 602 |
| Chain | Residue |
| C | ARG266 |
| C | PRO267 |
| C | THR350 |
| C | GLY351 |
| C | SER352 |
| C | GLY353 |
| C | LYS354 |
| C | THR355 |
| C | HIS356 |
| C | MG601 |
| C | HOH707 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue MG D 601 |
| Chain | Residue |
| D | THR355 |
| D | ADP602 |
| D | HOH701 |
| D | HOH710 |
| D | HOH712 |
| site_id | AD1 |
| Number of Residues | 12 |
| Details | binding site for residue ADP D 602 |
| Chain | Residue |
| D | ARG264 |
| D | ARG266 |
| D | GLN349 |
| D | GLY351 |
| D | SER352 |
| D | GLY353 |
| D | LYS354 |
| D | THR355 |
| D | HIS356 |
| D | MG601 |
| D | HOH701 |
| D | HOH706 |
Functional Information from PROSITE/UniProt
| site_id | PS00411 |
| Number of Residues | 12 |
| Details | KINESIN_MOTOR_1 Kinesin motor domain signature. GKFsLVDLAGNE |
| Chain | Residue | Details |
| A | GLY486-GLU497 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | Motif: {"description":"Nuclear localization signal","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 28 |
| Details | Binding site: {} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |