5A50
The crystal structure of Arabidopsis thaliana CAR4 in complex with two calcium ions, Zn and Phopho Choline
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005096 | molecular_function | GTPase activator activity |
| A | 0005509 | molecular_function | calcium ion binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005543 | molecular_function | phospholipid binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005829 | cellular_component | cytosol |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0008289 | molecular_function | lipid binding |
| A | 0009651 | biological_process | response to salt stress |
| A | 0009789 | biological_process | positive regulation of abscisic acid-activated signaling pathway |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 1900426 | biological_process | positive regulation of defense response to bacterium |
| A | 1901002 | biological_process | positive regulation of response to salt stress |
| B | 0005096 | molecular_function | GTPase activator activity |
| B | 0005509 | molecular_function | calcium ion binding |
| B | 0005515 | molecular_function | protein binding |
| B | 0005543 | molecular_function | phospholipid binding |
| B | 0005634 | cellular_component | nucleus |
| B | 0005829 | cellular_component | cytosol |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0008289 | molecular_function | lipid binding |
| B | 0009651 | biological_process | response to salt stress |
| B | 0009789 | biological_process | positive regulation of abscisic acid-activated signaling pathway |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 1900426 | biological_process | positive regulation of defense response to bacterium |
| B | 1901002 | biological_process | positive regulation of response to salt stress |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue CA A 201 |
| Chain | Residue |
| A | ARG50 |
| A | ASP51 |
| A | ASP102 |
| A | ASP104 |
| A | ASP110 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue CA A 202 |
| Chain | Residue |
| A | ASP104 |
| A | HOH353 |
| A | ASP51 |
| A | ASP56 |
| A | ASP102 |
| A | HIS103 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue CA B 201 |
| Chain | Residue |
| B | ASP51 |
| B | ASP56 |
| B | ASP102 |
| B | HIS103 |
| B | ASP104 |
| B | CA202 |
| B | HOH368 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue CA B 202 |
| Chain | Residue |
| B | ARG50 |
| B | ASP51 |
| B | ASP102 |
| B | ASP104 |
| B | ASP110 |
| B | CA201 |
| B | HOH371 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | binding site for residue PC B 203 |
| Chain | Residue |
| A | MET105 |
| B | TYR58 |
| B | VAL60 |
| B | LYS67 |
| B | LYS69 |
| B | TYR101 |
| B | GLY132 |
| B | HOH307 |
| B | HOH313 |
| B | HOH322 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 204 |
| Chain | Residue |
| B | HIS103 |
| B | ASP109 |
| B | ASP131 |
| B | PC205 |
| site_id | AC7 |
| Number of Residues | 13 |
| Details | binding site for residue PC B 205 |
| Chain | Residue |
| B | TYR58 |
| B | LYS69 |
| B | THR70 |
| B | ARG71 |
| B | VAL72 |
| B | HIS103 |
| B | ASP109 |
| B | GLN129 |
| B | LEU130 |
| B | ASP131 |
| B | ZN204 |
| B | HOH307 |
| B | HOH331 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"25465408","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4V29","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
