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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 16 |
| Details | binding site for residue ADP A 401 |
| Chain | Residue |
| A | ARG24 |
| A | PHE113 |
| A | GLU118 |
| A | MG402 |
| A | HOH503 |
| A | HOH510 |
| A | HOH521 |
| A | HOH565 |
| A | PRO27 |
| A | GLN106 |
| A | THR107 |
| A | GLY108 |
| A | THR109 |
| A | GLY110 |
| A | LYS111 |
| A | THR112 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 402 |
| Chain | Residue |
| A | THR112 |
| A | SER232 |
| A | ADP401 |
| A | HOH503 |
| A | HOH510 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | binding site for residue GCE A 403 |
| Chain | Residue |
| A | GLU116 |
| A | GLY117 |
| A | GLU118 |
| A | ARG119 |
| A | ALA133 |
| A | ILE136 |
| A | TYR211 |
| A | LEU214 |
| A | GLU215 |
| A | GLY217 |
| A | ALA218 |
| A | ARG221 |
| A | HOH530 |
| site_id | AC4 |
| Number of Residues | 16 |
| Details | binding site for residue ADP B 401 |
| Chain | Residue |
| B | ARG24 |
| B | ARG26 |
| B | PRO27 |
| B | GLN106 |
| B | THR107 |
| B | GLY108 |
| B | THR109 |
| B | GLY110 |
| B | LYS111 |
| B | THR112 |
| B | PHE113 |
| B | GLU118 |
| B | MG402 |
| B | HOH508 |
| B | HOH536 |
| B | HOH566 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue MG B 402 |
| Chain | Residue |
| B | THR112 |
| B | ADP401 |
| B | HOH508 |
| B | HOH536 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | binding site for residue GCE B 403 |
| Chain | Residue |
| B | GLU116 |
| B | GLY117 |
| B | GLU118 |
| B | ARG119 |
| B | ALA133 |
| B | ILE136 |
| B | TYR211 |
| B | GLY217 |
| B | ALA218 |
| B | ARG221 |
| site_id | AC7 |
| Number of Residues | 14 |
| Details | binding site for residue ADP C 401 |
| Chain | Residue |
| C | GLN106 |
| C | THR107 |
| C | GLY108 |
| C | THR109 |
| C | GLY110 |
| C | LYS111 |
| C | THR112 |
| C | PHE113 |
| C | GLU118 |
| C | HOH501 |
| C | HOH504 |
| C | HOH510 |
| C | HOH530 |
| C | HOH536 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue MG C 402 |
| Chain | Residue |
| C | THR112 |
| C | SER232 |
| C | HOH504 |
| C | HOH510 |
| C | HOH530 |
| site_id | AC9 |
| Number of Residues | 11 |
| Details | binding site for residue GCE C 403 |
| Chain | Residue |
| C | GLU116 |
| C | GLY117 |
| C | GLU118 |
| C | ALA133 |
| C | ILE136 |
| C | PRO137 |
| C | TYR211 |
| C | LEU214 |
| C | GLY217 |
| C | ALA218 |
| C | ARG221 |
Functional Information from PROSITE/UniProt
| site_id | PS00411 |
| Number of Residues | 12 |
| Details | KINESIN_MOTOR_1 Kinesin motor domain signature. GKLnLVDLAGSE |
| Chain | Residue | Details |
| A | GLY259-GLU270 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 21 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00283","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
