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 | 0003924 | molecular_function | GTPase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005525 | molecular_function | GTP binding |
A | 0005764 | cellular_component | lysosome |
A | 0005768 | cellular_component | endosome |
A | 0005770 | cellular_component | late endosome |
A | 0005783 | cellular_component | endoplasmic reticulum |
A | 0005789 | cellular_component | endoplasmic reticulum membrane |
A | 0005794 | cellular_component | Golgi apparatus |
A | 0005829 | cellular_component | cytosol |
A | 0005886 | cellular_component | plasma membrane |
A | 0015031 | biological_process | protein transport |
A | 0019003 | molecular_function | GDP binding |
A | 0030659 | cellular_component | cytoplasmic vesicle membrane |
A | 0030670 | cellular_component | phagocytic vesicle membrane |
A | 0032482 | biological_process | Rab protein signal transduction |
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 |
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 | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:25220469, ECO:0007744|PDB:4QXA |
Chain | Residue | Details |
A | GLY14 | |
A | ASN124 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | ASP62 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0007744|PDB:4QXA |
Chain | Residue | Details |
A | GLY65 | |
A | ALA155 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | MOD_RES: N-acetylalanine => ECO:0000250|UniProtKB:P51151 |
Chain | Residue | Details |
A | ALA2 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:21183079 |
Chain | Residue | Details |
A | SER34 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P51151 |
Chain | Residue | Details |
A | SER179 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P51151 |
Chain | Residue | Details |
A | THR187 |