4QXA
Crystal structure of the Rab9A-RUTBC2 RBD complex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000139 | cellular_component | Golgi membrane |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003924 | molecular_function | GTPase activity |
| A | 0003925 | molecular_function | G protein activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005525 | molecular_function | GTP binding |
| A | 0005764 | cellular_component | lysosome |
| A | 0005770 | cellular_component | late endosome |
| A | 0005789 | cellular_component | endoplasmic reticulum membrane |
| A | 0005829 | cellular_component | cytosol |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006898 | biological_process | receptor-mediated endocytosis |
| A | 0015031 | biological_process | protein transport |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0019003 | molecular_function | GDP binding |
| A | 0030659 | cellular_component | cytoplasmic vesicle membrane |
| A | 0030670 | cellular_component | phagocytic vesicle membrane |
| A | 0031410 | cellular_component | cytoplasmic vesicle |
| A | 0032482 | biological_process | Rab protein signal transduction |
| A | 0032880 | biological_process | regulation of protein localization |
| A | 0042147 | biological_process | retrograde transport, endosome to Golgi |
| A | 0042470 | cellular_component | melanosome |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0045335 | cellular_component | phagocytic vesicle |
| A | 0045921 | biological_process | positive regulation of exocytosis |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0005096 | molecular_function | GTPase activator activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE GTP A 301 |
| Chain | Residue |
| A | GLY16 |
| A | SER34 |
| A | GLN35 |
| A | LEU36 |
| A | HIS38 |
| A | THR39 |
| A | GLY65 |
| A | ASN124 |
| A | LYS125 |
| A | ASP127 |
| A | ILE128 |
| A | GLY17 |
| A | SER154 |
| A | ALA155 |
| A | LYS156 |
| A | MG302 |
| A | HOH411 |
| A | HOH416 |
| A | HOH424 |
| A | HOH425 |
| A | HOH447 |
| A | HOH452 |
| A | VAL18 |
| A | GLY19 |
| A | LYS20 |
| A | SER21 |
| A | SER22 |
| A | PHE32 |
| A | ASP33 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 302 |
| Chain | Residue |
| A | SER21 |
| A | THR39 |
| A | GTP301 |
| A | HOH446 |
| A | HOH447 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 11 |
| Details | Motif: {"description":"Switch 1","evidences":[{"source":"UniProtKB","id":"P51151","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 14 |
| Details | Motif: {"description":"Switch 2","evidences":[{"source":"UniProtKB","id":"P51151","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"25220469","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4QXA","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P51151","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"21183079","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 41 |
| Details | Region: {"description":"Important for interaction with RAB9A and RAB9B","evidences":[{"source":"PubMed","id":"25220469","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 49 |
| Details | Region: {"description":"Required for interaction with RAP family members","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
