6VIJ
Crystal structure of mouse RABL3 in complex with GDP
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0001779 | biological_process | natural killer cell differentiation |
A | 0003924 | molecular_function | GTPase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005525 | molecular_function | GTP binding |
A | 0006886 | biological_process | intracellular protein transport |
A | 0012505 | cellular_component | endomembrane system |
A | 0030183 | biological_process | B cell differentiation |
A | 0033077 | biological_process | T cell differentiation in thymus |
A | 0042803 | molecular_function | protein homodimerization activity |
A | 0046578 | biological_process | regulation of Ras protein signal transduction |
A | 0050821 | biological_process | protein stabilization |
A | 1903059 | biological_process | regulation of protein lipidation |
B | 0001779 | biological_process | natural killer cell differentiation |
B | 0003924 | molecular_function | GTPase activity |
B | 0005515 | molecular_function | protein binding |
B | 0005525 | molecular_function | GTP binding |
B | 0006886 | biological_process | intracellular protein transport |
B | 0012505 | cellular_component | endomembrane system |
B | 0030183 | biological_process | B cell differentiation |
B | 0033077 | biological_process | T cell differentiation in thymus |
B | 0042803 | molecular_function | protein homodimerization activity |
B | 0046578 | biological_process | regulation of Ras protein signal transduction |
B | 0050821 | biological_process | protein stabilization |
B | 1903059 | biological_process | regulation of protein lipidation |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | binding site for residue MG B 301 |
Chain | Residue |
B | SER20 |
B | THR38 |
B | GDP302 |
B | HOH410 |
B | HOH412 |
B | HOH423 |
site_id | AC2 |
Number of Residues | 20 |
Details | binding site for residue GDP B 302 |
Chain | Residue |
B | LYS19 |
B | SER20 |
B | SER21 |
B | PRO35 |
B | LYS148 |
B | ASP150 |
B | GLN151 |
B | ASP179 |
B | CYS180 |
B | MG301 |
B | HOH403 |
B | HOH410 |
B | HOH412 |
B | HOH423 |
B | HOH443 |
B | HOH445 |
B | HOH456 |
B | GLY16 |
B | VAL17 |
B | GLY18 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue MG A 301 |
Chain | Residue |
A | SER20 |
A | THR38 |
A | GDP302 |
A | HOH403 |
A | HOH405 |
A | HOH417 |
site_id | AC4 |
Number of Residues | 19 |
Details | binding site for residue GDP A 302 |
Chain | Residue |
A | GLY16 |
A | VAL17 |
A | GLY18 |
A | LYS19 |
A | SER20 |
A | SER21 |
A | PRO35 |
A | LYS148 |
A | ASP150 |
A | ASP179 |
A | CYS180 |
A | THR181 |
A | MG301 |
A | HOH403 |
A | HOH405 |
A | HOH417 |
A | HOH431 |
A | HOH441 |
A | HOH443 |
Functional Information from PROSITE/UniProt
site_id | PS00675 |
Number of Residues | 14 |
Details | SIGMA54_INTERACT_1 Sigma-54 interaction domain ATP-binding region A signature. VLVlGDSGVGKssL |
Chain | Residue | Details |
B | VAL9-LEU22 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:32220963, ECO:0007744|PDB:6VII, ECO:0007744|PDB:6VIJ |
Chain | Residue | Details |
B | GLY16 | |
B | LYS148 | |
B | ASP179 | |
A | GLY16 | |
A | LYS148 | |
A | ASP179 |