2J0V
The crystal structure of Arabidopsis thaliana RAC7-ROP9: the first RAS superfamily GTPase from the plant kingdom
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003924 | molecular_function | GTPase activity |
A | 0005525 | molecular_function | GTP binding |
A | 0005886 | cellular_component | plasma membrane |
A | 0007264 | biological_process | small GTPase-mediated signal transduction |
A | 0009738 | biological_process | abscisic acid-activated signaling pathway |
A | 0016020 | cellular_component | membrane |
B | 0003924 | molecular_function | GTPase activity |
B | 0005525 | molecular_function | GTP binding |
B | 0005886 | cellular_component | plasma membrane |
B | 0007264 | biological_process | small GTPase-mediated signal transduction |
B | 0009738 | biological_process | abscisic acid-activated signaling pathway |
B | 0016020 | cellular_component | membrane |
C | 0003924 | molecular_function | GTPase activity |
C | 0005525 | molecular_function | GTP binding |
C | 0005886 | cellular_component | plasma membrane |
C | 0007264 | biological_process | small GTPase-mediated signal transduction |
C | 0009738 | biological_process | abscisic acid-activated signaling pathway |
C | 0016020 | cellular_component | membrane |
D | 0003924 | molecular_function | GTPase activity |
D | 0005525 | molecular_function | GTP binding |
D | 0005886 | cellular_component | plasma membrane |
D | 0007264 | biological_process | small GTPase-mediated signal transduction |
D | 0009738 | biological_process | abscisic acid-activated signaling pathway |
D | 0016020 | cellular_component | membrane |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A1180 |
Chain | Residue |
A | THR20 |
A | THR38 |
A | GDP1179 |
A | HOH2027 |
A | HOH2069 |
A | HOH2073 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG B1183 |
Chain | Residue |
B | HOH2032 |
B | HOH2093 |
B | HOH2097 |
B | THR20 |
B | THR38 |
B | GDP1182 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG C1179 |
Chain | Residue |
C | THR20 |
C | THR38 |
C | GDP1178 |
C | HOH2021 |
C | HOH2058 |
C | HOH2059 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG D1181 |
Chain | Residue |
D | THR20 |
D | THR38 |
D | GDP1180 |
D | HOH2018 |
D | HOH2062 |
D | HOH2066 |
site_id | AC5 |
Number of Residues | 25 |
Details | BINDING SITE FOR RESIDUE GDP A1179 |
Chain | Residue |
A | ALA16 |
A | VAL17 |
A | GLY18 |
A | LYS19 |
A | THR20 |
A | CYS21 |
A | PHE31 |
A | ILE36 |
A | LYS119 |
A | ASP121 |
A | LEU122 |
A | SER157 |
A | SER158 |
A | LYS159 |
A | MG1180 |
A | HOH2027 |
A | HOH2057 |
A | HOH2069 |
A | HOH2070 |
A | HOH2071 |
A | HOH2072 |
A | HOH2073 |
B | ASP125 |
B | LYS126 |
B | GLY127 |
site_id | AC6 |
Number of Residues | 26 |
Details | BINDING SITE FOR RESIDUE GDP B1182 |
Chain | Residue |
A | ASP125 |
A | LYS126 |
A | GLY127 |
A | HOH2044 |
B | ALA16 |
B | VAL17 |
B | GLY18 |
B | LYS19 |
B | THR20 |
B | CYS21 |
B | PHE31 |
B | ILE36 |
B | LYS119 |
B | ASP121 |
B | LEU122 |
B | SER157 |
B | SER158 |
B | LYS159 |
B | MG1183 |
B | HOH2011 |
B | HOH2017 |
B | HOH2032 |
B | HOH2093 |
B | HOH2094 |
B | HOH2096 |
B | HOH2097 |
site_id | AC7 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE GDP C1178 |
Chain | Residue |
C | ALA16 |
C | VAL17 |
C | GLY18 |
C | LYS19 |
C | THR20 |
C | CYS21 |
C | PHE31 |
C | ILE36 |
C | LYS119 |
C | ASP121 |
C | LEU122 |
C | SER157 |
C | SER158 |
C | LYS159 |
C | MG1179 |
C | HOH2010 |
C | HOH2021 |
C | HOH2051 |
C | HOH2057 |
C | HOH2058 |
C | HOH2059 |
D | ASP125 |
D | LYS126 |
D | GLY127 |
site_id | AC8 |
Number of Residues | 25 |
Details | BINDING SITE FOR RESIDUE GDP D1180 |
Chain | Residue |
C | ASP125 |
C | LYS126 |
C | GLY127 |
D | ALA16 |
D | VAL17 |
D | GLY18 |
D | LYS19 |
D | THR20 |
D | CYS21 |
D | PHE31 |
D | ILE36 |
D | LYS119 |
D | ASP121 |
D | LEU122 |
D | SER157 |
D | SER158 |
D | LYS159 |
D | MG1181 |
D | HOH2018 |
D | HOH2055 |
D | HOH2062 |
D | HOH2063 |
D | HOH2064 |
D | HOH2065 |
D | HOH2066 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | GLY13 | |
A | ASP60 | |
A | THR118 | |
B | GLY13 | |
B | ASP60 | |
B | THR118 | |
C | GLY13 | |
C | ASP60 | |
C | THR118 | |
D | GLY13 | |
D | ASP60 | |
D | THR118 |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | LIPID: S-palmitoyl cysteine => ECO:0000305|PubMed:12368496 |
Chain | Residue | Details |
A | CYS196 | |
A | CYS203 | |
A | CYS206 | |
B | CYS196 | |
B | CYS203 | |
B | CYS206 | |
C | CYS196 | |
C | CYS203 | |
C | CYS206 | |
D | CYS196 | |
D | CYS203 | |
D | CYS206 |