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 | 22 |
| Details | binding site for residue ANP B 401 |
| Chain | Residue |
| B | ARG11 |
| B | SER110 |
| B | TYR111 |
| B | SER220 |
| B | GLY256 |
| B | MG402 |
| B | HOH538 |
| B | HOH547 |
| B | HOH553 |
| B | HOH572 |
| B | HOH576 |
| B | ARG13 |
| B | HOH582 |
| B | HOH629 |
| B | HOH655 |
| B | PRO14 |
| B | GLN104 |
| B | THR105 |
| B | GLY106 |
| B | SER107 |
| B | GLY108 |
| B | LYS109 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue MG B 402 |
| Chain | Residue |
| B | SER110 |
| B | ANP401 |
| B | HOH538 |
| B | HOH553 |
| B | HOH576 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue MG B 403 |
| Chain | Residue |
| B | TYR95 |
| B | ASN96 |
| B | ASN321 |
| B | VAL358 |
| B | ASN360 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue PO4 B 404 |
| Chain | Residue |
| B | SER342 |
| B | ARG345 |
| B | ARG349 |
| B | HOH520 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue PO4 B 405 |
| Chain | Residue |
| B | LYS54 |
| B | ARG345 |
| B | HOH517 |
| site_id | AC6 |
| Number of Residues | 22 |
| Details | binding site for residue ANP A 401 |
| Chain | Residue |
| A | ARG11 |
| A | PRO14 |
| A | SER64 |
| A | GLN104 |
| A | THR105 |
| A | GLY106 |
| A | SER107 |
| A | GLY108 |
| A | LYS109 |
| A | SER110 |
| A | TYR111 |
| A | SER220 |
| A | GLY256 |
| A | MG402 |
| A | HOH509 |
| A | HOH520 |
| A | HOH541 |
| A | HOH552 |
| A | HOH586 |
| A | HOH588 |
| A | HOH605 |
| A | HOH619 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 402 |
| Chain | Residue |
| A | SER110 |
| A | ANP401 |
| A | HOH520 |
| A | HOH541 |
| A | HOH586 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue PO4 A 403 |
| Chain | Residue |
| A | SER342 |
| A | ARG345 |
| A | HOH539 |
| site_id | AC9 |
| Number of Residues | 21 |
| Details | binding site for residue ANP C 401 |
| Chain | Residue |
| C | ARG11 |
| C | ARG13 |
| C | PRO14 |
| C | SER64 |
| C | THR105 |
| C | GLY106 |
| C | SER107 |
| C | GLY108 |
| C | LYS109 |
| C | SER110 |
| C | TYR111 |
| C | SER220 |
| C | GLY256 |
| C | MG402 |
| C | HOH505 |
| C | HOH516 |
| C | HOH525 |
| C | HOH538 |
| C | HOH541 |
| C | HOH565 |
| C | HOH571 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue MG C 402 |
| Chain | Residue |
| C | SER110 |
| C | ANP401 |
| C | HOH516 |
| C | HOH538 |
| C | HOH571 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue MG C 403 |
| Chain | Residue |
| C | ASN360 |
| C | TYR95 |
| C | ASN96 |
| C | ASN321 |
| C | VAL358 |
Functional Information from PROSITE/UniProt
| site_id | PS00411 |
| Number of Residues | 12 |
| Details | KINESIN_MOTOR_1 Kinesin motor domain signature. GKLsLVDLAGSE |
| Chain | Residue | Details |
| B | GLY247-GLU258 | |
