3SH0
Crystal Structure of E. coli undecaprenyl pyrophosphate synthase in complex with BPH-1065
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0008360 | biological_process | regulation of cell shape |
| A | 0008834 | molecular_function | di-trans,poly-cis-undecaprenyl-diphosphate synthase activity |
| A | 0009252 | biological_process | peptidoglycan biosynthetic process |
| A | 0016094 | biological_process | polyprenol biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016765 | molecular_function | transferase activity, transferring alkyl or aryl (other than methyl) groups |
| A | 0036094 | molecular_function | small molecule binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0043164 | biological_process | Gram-negative-bacterium-type cell wall biogenesis |
| A | 0045547 | molecular_function | dehydrodolichyl diphosphate synthase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051301 | biological_process | cell division |
| A | 0071555 | biological_process | cell wall organization |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0008360 | biological_process | regulation of cell shape |
| B | 0008834 | molecular_function | di-trans,poly-cis-undecaprenyl-diphosphate synthase activity |
| B | 0009252 | biological_process | peptidoglycan biosynthetic process |
| B | 0016094 | biological_process | polyprenol biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016765 | molecular_function | transferase activity, transferring alkyl or aryl (other than methyl) groups |
| B | 0036094 | molecular_function | small molecule binding |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0043164 | biological_process | Gram-negative-bacterium-type cell wall biogenesis |
| B | 0045547 | molecular_function | dehydrodolichyl diphosphate synthase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051301 | biological_process | cell division |
| B | 0071555 | biological_process | cell wall organization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE SAX B 1001 |
| Chain | Residue |
| B | ALA47 |
| B | HOH357 |
| B | HOH407 |
| B | LEU85 |
| B | MET86 |
| B | ILE141 |
| B | ALA142 |
| B | ALA143 |
| B | ASN144 |
| B | HOH299 |
| B | HOH310 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SAX B 1002 |
| Chain | Residue |
| B | SER55 |
| B | ALA58 |
| B | ASN59 |
| B | SER99 |
| B | LEU100 |
| B | HIS103 |
| B | HOH272 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SAX A 2001 |
| Chain | Residue |
| A | VAL50 |
| A | SER55 |
| A | ALA58 |
| A | ASN59 |
| A | LEU93 |
| A | GLU96 |
| A | SER99 |
| A | HIS103 |
| A | LEU107 |
Functional Information from PROSITE/UniProt
| site_id | PS01066 |
| Number of Residues | 18 |
| Details | UPP_SYNTHASE Undecaprenyl pyrophosphate synthase family signature. DLVIRTGGehRiSnFLLW |
| Chain | Residue | Details |
| B | ASP190-TRP207 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: |
| Chain | Residue | Details |
| B | ASP26 | |
| A | ASP26 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000250 |
| Chain | Residue | Details |
| B | ASN74 | |
| A | ASN74 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | BINDING: |
| Chain | Residue | Details |
| B | ASP26 | |
| B | HIS199 | |
| B | ARG200 | |
| B | GLU213 | |
| A | ASP26 | |
| A | HIS199 | |
| A | ARG200 | |
| A | GLU213 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:15044730 |
| Chain | Residue | Details |
| B | TRP31 | |
| B | TRP75 | |
| A | TRP31 | |
| A | TRP75 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15044730 |
| Chain | Residue | Details |
| B | ARG39 | |
| B | HIS43 | |
| B | ARG77 | |
| B | ARG194 | |
| A | ARG39 | |
| A | HIS43 | |
| A | ARG77 | |
| A | ARG194 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| B | SER71 | |
| A | SER71 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | SITE: Required for continued chain elongation |
| Chain | Residue | Details |
| B | ALA69 | |
| A | ALA69 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | SITE: Important for determining product length |
| Chain | Residue | Details |
| B | LEU137 | |
| A | LEU137 |
