3HXD
Engineered RabGGTase in complex with a peptidomimetic inhibitor (compound 9)
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0008318 | molecular_function | protein prenyltransferase activity |
A | 0018342 | biological_process | protein prenylation |
B | 0003824 | molecular_function | catalytic activity |
B | 0004659 | molecular_function | prenyltransferase activity |
B | 0004661 | molecular_function | protein geranylgeranyltransferase activity |
B | 0004663 | molecular_function | Rab geranylgeranyltransferase activity |
B | 0005515 | molecular_function | protein binding |
B | 0005968 | cellular_component | Rab-protein geranylgeranyltransferase complex |
B | 0006888 | biological_process | endoplasmic reticulum to Golgi vesicle-mediated transport |
B | 0008270 | molecular_function | zinc ion binding |
B | 0008318 | molecular_function | protein prenyltransferase activity |
B | 0018344 | biological_process | protein geranylgeranylation |
B | 0019840 | molecular_function | isoprenoid binding |
B | 0031267 | molecular_function | small GTPase binding |
B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 332 |
Chain | Residue |
B | ASP238 |
B | CYS240 |
B | HIS290 |
B | BD7334 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA B 333 |
Chain | Residue |
B | HOH509 |
A | ALA138 |
A | HOH400 |
B | HIS64 |
B | MET66 |
B | HOH415 |
site_id | AC3 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE BD7 B 334 |
Chain | Residue |
B | TRP52 |
B | LEU96 |
B | ARG144 |
B | PHE147 |
B | CYS148 |
B | GLY192 |
B | GLN193 |
B | CYS196 |
B | ASP238 |
B | TYR241 |
B | TRP244 |
B | PHE289 |
B | HIS290 |
B | ZN332 |
B | HOH373 |
B | HOH380 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:18756270, ECO:0007744|PDB:3DST, ECO:0007744|PDB:3DSX |
Chain | Residue | Details |
B | HIS190 |
site_id | SWS_FT_FI2 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000269|PubMed:18399557, ECO:0000269|PubMed:18756270, ECO:0000269|PubMed:19894725, ECO:0000269|PubMed:22480322, ECO:0000269|PubMed:22963166 |
Chain | Residue | Details |
B | ASP238 | |
B | CYS240 | |
B | HIS290 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0007744|PDB:3DST, ECO:0007744|PDB:3DSV |
Chain | Residue | Details |
B | TYR241 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | MOD_RES: N-acetylglycine => ECO:0000250|UniProtKB:P53611 |
Chain | Residue | Details |
B | GLY2 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P53611 |
Chain | Residue | Details |
B | THR3 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1d8d |
Chain | Residue | Details |
B | TYR241 |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1d8d |
Chain | Residue | Details |
A | LYS105 |