3PZ1
Crystal structure of RabGGTase(DELTA LRR; DELTA IG) in Complex with BMS3
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 | 9 |
| Details | BINDING SITE FOR RESIDUE 3PZ B 1 |
| Chain | Residue |
| B | TYR44 |
| B | LEU45 |
| B | ASP238 |
| B | PHE289 |
| B | HIS290 |
| B | ZN332 |
| B | DMS334 |
| B | DMS335 |
| B | DMS336 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 332 |
| Chain | Residue |
| B | 3PZ1 |
| B | ASP238 |
| B | CYS240 |
| B | HIS290 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 333 |
| Chain | Residue |
| A | ALA138 |
| B | HIS64 |
| B | MET66 |
| B | HOH346 |
| B | HOH477 |
| B | HOH534 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE DMS B 334 |
| Chain | Residue |
| A | TYR107 |
| B | 3PZ1 |
| B | ARG144 |
| B | HIS190 |
| B | GLY192 |
| B | GLN193 |
| B | DMS336 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE DMS B 335 |
| Chain | Residue |
| B | 3PZ1 |
| B | TYR241 |
| B | TRP244 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE DMS B 336 |
| Chain | Residue |
| B | 3PZ1 |
| B | LEU96 |
| B | ARG144 |
| B | CYS196 |
| B | TRP244 |
| B | DMS334 |
| B | HOH475 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE DMS B 337 |
| Chain | Residue |
| B | TYR195 |
| B | TRP243 |
| B | TRP244 |
| B | CYS314 |
| B | HOH375 |
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 |
