6VII
Crystal structure of mouse RABL3 in complex with GTPgammaS
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0001779 | biological_process | natural killer cell differentiation |
| A | 0005515 | molecular_function | protein binding |
| A | 0005525 | molecular_function | GTP binding |
| 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 | 0005515 | molecular_function | protein binding |
| B | 0005525 | molecular_function | GTP binding |
| 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 | 5 |
| Details | binding site for residue MG B 301 |
| Chain | Residue |
| B | SER20 |
| B | THR38 |
| B | GSP302 |
| B | HOH411 |
| B | HOH423 |
| site_id | AC2 |
| Number of Residues | 21 |
| Details | binding site for residue GSP B 302 |
| Chain | Residue |
| B | LYS19 |
| B | SER20 |
| B | SER21 |
| B | PRO35 |
| B | THR38 |
| B | LYS148 |
| B | ASP150 |
| B | GLN151 |
| B | ASP179 |
| B | CYS180 |
| B | THR181 |
| B | MG301 |
| B | HOH407 |
| B | HOH411 |
| B | HOH412 |
| B | HOH423 |
| B | HOH428 |
| B | SER15 |
| B | GLY16 |
| B | VAL17 |
| B | GLY18 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 301 |
| Chain | Residue |
| A | SER20 |
| A | THR38 |
| A | GSP302 |
| A | HOH404 |
| A | HOH412 |
| site_id | AC4 |
| Number of Residues | 22 |
| Details | binding site for residue GSP A 302 |
| Chain | Residue |
| A | SER15 |
| A | GLY16 |
| A | VAL17 |
| A | GLY18 |
| A | LYS19 |
| A | SER20 |
| A | SER21 |
| A | PRO35 |
| A | THR38 |
| A | LYS148 |
| A | ASP150 |
| A | ASP179 |
| A | CYS180 |
| A | THR181 |
| A | MG301 |
| A | HOH402 |
| A | HOH404 |
| A | HOH407 |
| A | HOH412 |
| A | HOH414 |
| A | HOH434 |
| A | HOH452 |
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 |
