4MIT
Crystal structure of E. histolytica RacC bound to the EhPAK4 PBD
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003924 | molecular_function | GTPase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005525 | molecular_function | GTP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005856 | cellular_component | cytoskeleton |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0007015 | biological_process | actin filament organization |
| A | 0007163 | biological_process | establishment or maintenance of cell polarity |
| A | 0007165 | biological_process | signal transduction |
| A | 0007264 | biological_process | small GTPase-mediated signal transduction |
| A | 0008360 | biological_process | regulation of cell shape |
| A | 0016020 | cellular_component | membrane |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0019901 | molecular_function | protein kinase binding |
| A | 0030865 | biological_process | cortical cytoskeleton organization |
| A | 0031410 | cellular_component | cytoplasmic vesicle |
| A | 0032956 | biological_process | regulation of actin cytoskeleton organization |
| A | 0042995 | cellular_component | cell projection |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003924 | molecular_function | GTPase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005525 | molecular_function | GTP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005856 | cellular_component | cytoskeleton |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0007015 | biological_process | actin filament organization |
| B | 0007163 | biological_process | establishment or maintenance of cell polarity |
| B | 0007165 | biological_process | signal transduction |
| B | 0007264 | biological_process | small GTPase-mediated signal transduction |
| B | 0008360 | biological_process | regulation of cell shape |
| B | 0016020 | cellular_component | membrane |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0019901 | molecular_function | protein kinase binding |
| B | 0030865 | biological_process | cortical cytoskeleton organization |
| B | 0031410 | cellular_component | cytoplasmic vesicle |
| B | 0032956 | biological_process | regulation of actin cytoskeleton organization |
| B | 0042995 | cellular_component | cell projection |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0003924 | molecular_function | GTPase activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005525 | molecular_function | GTP binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005856 | cellular_component | cytoskeleton |
| C | 0005886 | cellular_component | plasma membrane |
| C | 0007015 | biological_process | actin filament organization |
| C | 0007163 | biological_process | establishment or maintenance of cell polarity |
| C | 0007165 | biological_process | signal transduction |
| C | 0007264 | biological_process | small GTPase-mediated signal transduction |
| C | 0008360 | biological_process | regulation of cell shape |
| C | 0016020 | cellular_component | membrane |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0019901 | molecular_function | protein kinase binding |
| C | 0030865 | biological_process | cortical cytoskeleton organization |
| C | 0031410 | cellular_component | cytoplasmic vesicle |
| C | 0032956 | biological_process | regulation of actin cytoskeleton organization |
| C | 0042995 | cellular_component | cell projection |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0003924 | molecular_function | GTPase activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0005525 | molecular_function | GTP binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005856 | cellular_component | cytoskeleton |
| D | 0005886 | cellular_component | plasma membrane |
| D | 0007015 | biological_process | actin filament organization |
| D | 0007163 | biological_process | establishment or maintenance of cell polarity |
| D | 0007165 | biological_process | signal transduction |
| D | 0007264 | biological_process | small GTPase-mediated signal transduction |
| D | 0008360 | biological_process | regulation of cell shape |
| D | 0016020 | cellular_component | membrane |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0019901 | molecular_function | protein kinase binding |
| D | 0030865 | biological_process | cortical cytoskeleton organization |
| D | 0031410 | cellular_component | cytoplasmic vesicle |
| D | 0032956 | biological_process | regulation of actin cytoskeleton organization |
| D | 0042995 | cellular_component | cell projection |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE GTP A 201 |
| Chain | Residue |
| A | GLY19 |
| A | TYR39 |
| A | PRO41 |
| A | THR42 |
| A | GLY67 |
| A | LYS123 |
| A | ASP125 |
| A | THR126 |
| A | SER165 |
| A | ALA166 |
| A | LYS167 |
| A | ALA20 |
| A | MG202 |
| A | HOH305 |
| A | HOH306 |
| A | HOH309 |
| A | HOH313 |
| A | HOH317 |
| A | VAL21 |
| A | GLY22 |
| A | LYS23 |
| A | THR24 |
| A | CYS25 |
| A | PHE35 |
| A | GLU37 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 202 |
| Chain | Residue |
| A | THR24 |
| A | THR42 |
| A | GTP201 |
| A | HOH305 |
| A | HOH306 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 203 |
| Chain | Residue |
| A | ASP72 |
| A | HOH327 |
| A | HOH328 |
| A | HOH329 |
| A | HOH356 |
| A | HOH360 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG A 204 |
| Chain | Residue |
| A | ALA112 |
| A | PRO113 |
| A | LYS114 |
| site_id | AC5 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE GTP B 201 |
| Chain | Residue |
| B | ALA20 |
| B | VAL21 |
| B | GLY22 |
| B | LYS23 |
| B | THR24 |
| B | CYS25 |
| B | PHE35 |
| B | GLU37 |
| B | TYR39 |
| B | PRO41 |
| B | THR42 |
| B | GLY67 |
| B | LYS123 |
| B | ASP125 |
| B | THR126 |
| B | SER165 |
| B | ALA166 |
| B | LYS167 |
| B | MG202 |
| B | HOH303 |
| B | HOH304 |
| B | HOH305 |
| B | HOH307 |
| B | HOH311 |
| B | HOH312 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 202 |
| Chain | Residue |
| B | THR24 |
| B | THR42 |
| B | GTP201 |
| B | HOH303 |
| B | HOH304 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 203 |
| Chain | Residue |
| B | ASP72 |
| B | HOH331 |
| B | HOH332 |
| B | HOH333 |
| B | HOH334 |
| B | HOH353 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG B 204 |
| Chain | Residue |
| B | ALA112 |
| B | LYS114 |
| site_id | AC9 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE GTP C 201 |
| Chain | Residue |
| C | HOH315 |
| C | HOH357 |
| C | HOH358 |
| C | HOH360 |
| C | HOH363 |
| C | GLY19 |
| C | ALA20 |
| C | VAL21 |
| C | GLY22 |
| C | LYS23 |
| C | THR24 |
| C | CYS25 |
| C | PHE35 |
| C | GLU37 |
| C | TYR39 |
| C | PRO41 |
| C | THR42 |
| C | GLY67 |
| C | LYS123 |
| C | ASP125 |
| C | THR126 |
| C | SER165 |
| C | ALA166 |
| C | LYS167 |
| C | MG202 |
| C | HOH303 |
| C | HOH304 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG C 202 |
| Chain | Residue |
| C | THR24 |
| C | THR42 |
| C | GTP201 |
| C | HOH303 |
| C | HOH304 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG C 203 |
| Chain | Residue |
| C | ASP72 |
| C | HOH320 |
| C | HOH327 |
| C | HOH332 |
| C | HOH341 |
| site_id | BC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG C 204 |
| Chain | Residue |
| C | ALA112 |
| C | PRO113 |
| C | LYS114 |
| site_id | BC4 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE GTP D 201 |
| Chain | Residue |
| D | GLY19 |
| D | ALA20 |
| D | VAL21 |
| D | GLY22 |
| D | LYS23 |
| D | THR24 |
| D | CYS25 |
| D | PHE35 |
| D | GLU37 |
| D | TYR39 |
| D | PRO41 |
| D | THR42 |
| D | GLY67 |
| D | LYS123 |
| D | ASP125 |
| D | THR126 |
| D | SER165 |
| D | ALA166 |
| D | LYS167 |
| D | MG202 |
| D | HOH302 |
| D | HOH313 |
| D | HOH314 |
| D | HOH319 |
| D | HOH339 |
| site_id | BC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG D 202 |
| Chain | Residue |
| D | THR24 |
| D | THR42 |
| D | GTP201 |
| D | HOH302 |
| D | HOH341 |
| site_id | BC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG D 203 |
| Chain | Residue |
| D | ASP72 |
| D | HOH303 |
| D | HOH304 |
| D | HOH328 |
| D | HOH357 |
| site_id | BC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG D 204 |
| Chain | Residue |
| D | ALA112 |
| D | PRO113 |
| D | LYS114 |
| D | VAL115 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 52 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:25529118, ECO:0007744|PDB:4MIT |
| Chain | Residue | Details |
| A | ALA20 | |
| A | LYS123 | |
| A | ASP125 | |
| A | ALA166 | |
| A | LYS167 | |
| B | ALA20 | |
| B | GLY22 | |
| B | LYS23 | |
| B | THR24 | |
| B | CYS25 | |
| B | GLU37 | |
| A | GLY22 | |
| B | TYR39 | |
| B | THR42 | |
| B | GLY67 | |
| B | LYS123 | |
| B | ASP125 | |
| B | ALA166 | |
| B | LYS167 | |
| C | ALA20 | |
| C | GLY22 | |
| C | LYS23 | |
| A | LYS23 | |
| C | THR24 | |
| C | CYS25 | |
| C | GLU37 | |
| C | TYR39 | |
| C | THR42 | |
| C | GLY67 | |
| C | LYS123 | |
| C | ASP125 | |
| C | ALA166 | |
| C | LYS167 | |
| A | THR24 | |
| D | ALA20 | |
| D | GLY22 | |
| D | LYS23 | |
| D | THR24 | |
| D | CYS25 | |
| D | GLU37 | |
| D | TYR39 | |
| D | THR42 | |
| D | GLY67 | |
| D | LYS123 | |
| A | CYS25 | |
| D | ASP125 | |
| D | ALA166 | |
| D | LYS167 | |
| A | GLU37 | |
| A | TYR39 | |
| A | THR42 | |
| A | GLY67 |
