4DBP
Myosin VI nucleotide-free (MDINSERT2) D179Y crystal structure
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003774 | molecular_function | cytoskeletal motor activity |
A | 0005524 | molecular_function | ATP binding |
A | 0016459 | cellular_component | myosin complex |
A | 0051015 | molecular_function | actin filament binding |
C | 0005509 | molecular_function | calcium ion binding |
C | 0005515 | molecular_function | protein binding |
C | 0005654 | cellular_component | nucleoplasm |
C | 0005737 | cellular_component | cytoplasm |
C | 0005813 | cellular_component | centrosome |
C | 0005814 | cellular_component | centriole |
C | 0005819 | cellular_component | spindle |
C | 0005829 | cellular_component | cytosol |
C | 0005886 | cellular_component | plasma membrane |
C | 0005938 | cellular_component | cell cortex |
C | 0006468 | biological_process | protein phosphorylation |
C | 0007099 | biological_process | centriole replication |
C | 0007605 | biological_process | sensory perception of sound |
C | 0007608 | biological_process | sensory perception of smell |
C | 0016028 | cellular_component | rhabdomere |
C | 0016056 | biological_process | rhodopsin mediated signaling pathway |
C | 0016059 | biological_process | negative regulation of opsin-mediated signaling pathway |
C | 0016060 | biological_process | metarhodopsin inactivation |
C | 0016062 | biological_process | obsolete adaptation of rhodopsin mediated signaling |
C | 0016247 | molecular_function | channel regulator activity |
C | 0030048 | biological_process | actin filament-based movement |
C | 0030234 | molecular_function | enzyme regulator activity |
C | 0030496 | cellular_component | midbody |
C | 0031475 | cellular_component | myosin V complex |
C | 0031476 | cellular_component | myosin VI complex |
C | 0031477 | cellular_component | myosin VII complex |
C | 0031489 | molecular_function | myosin V binding |
C | 0032036 | molecular_function | myosin heavy chain binding |
C | 0042052 | biological_process | rhabdomere development |
C | 0046716 | biological_process | muscle cell cellular homeostasis |
C | 0046872 | molecular_function | metal ion binding |
C | 0048102 | biological_process | autophagic cell death |
C | 0050911 | biological_process | detection of chemical stimulus involved in sensory perception of smell |
C | 0051383 | biological_process | kinetochore organization |
C | 0070855 | molecular_function | myosin VI head/neck binding |
C | 0071361 | biological_process | cellular response to ethanol |
C | 0072499 | biological_process | photoreceptor cell axon guidance |
C | 0072686 | cellular_component | mitotic spindle |
C | 0097431 | cellular_component | mitotic spindle pole |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE TBU A 901 |
Chain | Residue |
A | ARG205 |
A | PHE206 |
A | LEU229 |
A | HOH1528 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE TBU A 902 |
Chain | Residue |
A | THR158 |
A | LEU165 |
A | ASN186 |
A | LYS208 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 903 |
Chain | Residue |
A | LYS720 |
A | ASP767 |
A | LYS771 |
A | MET717 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 904 |
Chain | Residue |
A | ASN284 |
A | ASP288 |
A | GLY304 |
A | SER305 |
A | HOH1454 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO A 905 |
Chain | Residue |
A | ARG487 |
A | HOH1482 |
A | HOH1599 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO A 906 |
Chain | Residue |
A | TYR100 |
A | LYS670 |
A | LEU673 |
A | HOH1114 |
A | HOH1511 |
A | HOH1547 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 907 |
Chain | Residue |
A | LYS550 |
A | HIS551 |
A | ASP553 |
A | HIS554 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 908 |
Chain | Residue |
A | VAL7 |
A | PRO50 |
A | HOH1345 |
A | HOH1584 |
site_id | AC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 909 |
Chain | Residue |
A | LYS142 |
A | LEU143 |
A | SER144 |
A | SER449 |
A | HOH1406 |
site_id | BC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO A 910 |
Chain | Residue |
A | ARG556 |
A | HIS581 |
A | PHE582 |
site_id | BC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 911 |
Chain | Residue |
A | PRO50 |
A | LEU68 |
A | ASN69 |
A | GLY761 |
A | HOH1588 |
site_id | BC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO A 912 |
Chain | Residue |
A | ALA253 |
A | GLY254 |
A | ALA255 |
A | GLN290 |
A | ILE291 |
A | LEU292 |
A | ARG295 |
A | HIS314 |
site_id | BC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 913 |
Chain | Residue |
A | ASN275 |
A | THR279 |
A | GLU299 |
A | HOH1034 |
site_id | BC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO A 914 |
Chain | Residue |
A | THR197 |
A | VAL198 |
A | ARG205 |
A | GLU242 |
A | GLU461 |
A | PHE463 |
A | HOH1045 |
site_id | BC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO A 915 |
Chain | Residue |
A | LYS232 |
A | SER233 |
A | HOH1528 |
site_id | BC7 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE EDO A 916 |
Chain | Residue |
A | GLU505 |
A | HIS507 |
site_id | BC8 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO A 917 |
Chain | Residue |
A | GLY173 |
A | THR174 |
A | GLY175 |
A | GLN176 |
A | ASP177 |
A | ILE178 |
A | VAL220 |
site_id | BC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 918 |
Chain | Residue |
A | GLU231 |
A | SER233 |
A | ARG234 |
A | VAL237 |
A | HOH1216 |
site_id | CC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO A 919 |
Chain | Residue |
A | LYS498 |
C | PHE65 |
C | PRO66 |
site_id | CC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 920 |
Chain | Residue |
A | PHE49 |
A | ASN69 |
A | GLU70 |
A | ASP699 |
A | GLN702 |
site_id | CC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE IPA A 921 |
Chain | Residue |
A | ASN477 |
A | GLN481 |
A | ARG667 |
A | SER692 |
A | HOH1239 |
A | HOH1583 |
site_id | CC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA C 201 |
Chain | Residue |
C | ASP24 |
C | THR26 |
C | GLU31 |
C | HOH303 |
C | ASP20 |
C | ASP22 |
site_id | CC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA C 202 |
Chain | Residue |
C | ASP56 |
C | ASP58 |
C | ASN60 |
C | THR62 |
C | GLU67 |
site_id | CC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA C 203 |
Chain | Residue |
C | ASP93 |
C | ASP95 |
C | ASN97 |
C | PHE99 |
C | GLU104 |
site_id | CC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA C 204 |
Chain | Residue |
C | ASP129 |
C | ASP131 |
C | ASP133 |
C | GLN135 |
C | GLU140 |
Functional Information from PROSITE/UniProt
site_id | PS00018 |
Number of Residues | 13 |
Details | EF_HAND_1 EF-hand calcium-binding domain. DKDGDGTITtkEL |
Chain | Residue | Details |
C | ASP20-LEU32 | |
C | ASP56-PHE68 | |
C | ASP93-LEU105 | |
C | ASP129-PHE141 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000255 |
Chain | Residue | Details |
A | GLY151 | |
C | GLU67 | |
C | ASP93 | |
C | ASP95 | |
C | ASN97 | |
C | GLU104 | |
C | ASP129 | |
C | ASP131 | |
C | ASP133 | |
C | GLN135 | |
C | GLU140 | |
C | ASP22 | |
C | ASP24 | |
C | THR26 | |
C | GLU31 | |
C | ASP56 | |
C | ASP58 | |
C | ASN60 | |
C | THR62 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9UM54 |
Chain | Residue | Details |
A | SER267 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine => ECO:0000269|PubMed:12682054 |
Chain | Residue | Details |
A | VAL406 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q64331 |
Chain | Residue | Details |
A | LEU605 |