3PZ2
Crystal structure of RabGGTase(DELTA LRR; DELTA IG) in Complex with BMS3 and lipid substrate GGPP
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 | 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 1 |
| Chain | Residue |
| B | ASP238 |
| B | CYS240 |
| B | HIS290 |
| B | 3PZ333 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA B 332 |
| Chain | Residue |
| A | ALA138 |
| A | HOH355 |
| B | HIS64 |
| B | MET66 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE 3PZ B 333 |
| Chain | Residue |
| B | TYR44 |
| B | LEU45 |
| B | ASP238 |
| B | ASP287 |
| B | PRO288 |
| B | PHE289 |
| B | HIS290 |
| B | GRG334 |
| B | HOH375 |
| B | ZN1 |
| site_id | AC4 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE GRG B 334 |
| Chain | Residue |
| A | LYS105 |
| A | PHE143 |
| A | HOH344 |
| B | TYR51 |
| B | LEU96 |
| B | GLN103 |
| B | ARG144 |
| B | PHE147 |
| B | HIS190 |
| B | GLY192 |
| B | GLN193 |
| B | TYR195 |
| B | CYS196 |
| B | ARG232 |
| B | LYS235 |
| B | CYS240 |
| B | TYR241 |
| B | PHE293 |
| B | 3PZ333 |
| B | HOH346 |
| B | HOH352 |
| B | HOH375 |
| B | HOH392 |
| B | HOH396 |
| B | HOH397 |
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 | CYS240 | |
| B | HIS290 | |
| B | ASP238 |
| 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 |
