3SGV
Crystal Structure of E. coli undecaprenyl pyrophosphate synthase in complex with BPH-1290
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 | 19 |
Details | BINDING SITE FOR RESIDUE 2BJ A 2001 |
Chain | Residue |
A | ILE24 |
A | ALA69 |
A | PHE70 |
A | SER71 |
A | GLU73 |
A | ASN74 |
A | ARG194 |
A | HOH286 |
A | HOH342 |
A | 2BJ3001 |
A | 2BJ4001 |
A | MET25 |
A | ASP26 |
A | GLY27 |
A | ASN28 |
A | GLY29 |
A | ARG39 |
A | HIS43 |
A | TYR68 |
site_id | AC2 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE 2BJ A 3001 |
Chain | Residue |
A | MET25 |
A | LEU67 |
A | ALA69 |
A | PHE70 |
A | TRP75 |
A | MET86 |
A | PHE89 |
A | GLU96 |
A | PHE116 |
A | ILE141 |
A | ALA142 |
A | ALA143 |
A | ASN144 |
A | HOH266 |
A | HOH274 |
A | HOH368 |
A | 2BJ2001 |
A | 2BJ4001 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE 2BJ A 4001 |
Chain | Residue |
A | HIS43 |
A | TRP75 |
A | 2BJ2001 |
A | 2BJ3001 |
site_id | AC4 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE 2BJ B 5001 |
Chain | Residue |
A | GLN163 |
B | HIS43 |
B | LYS44 |
B | ALA47 |
B | LYS48 |
B | VAL50 |
B | ARG51 |
B | LEU88 |
B | ALA92 |
B | GLU96 |
B | GLN168 |
B | HOH268 |
B | HOH371 |
B | 2BJ1001 |
site_id | AC5 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE 2BJ B 1001 |
Chain | Residue |
B | MET25 |
B | ASP26 |
B | GLY27 |
B | ASN28 |
B | GLY29 |
B | HIS43 |
B | VAL50 |
B | ALA69 |
B | LEU85 |
B | PHE89 |
B | HOH284 |
B | HOH340 |
B | 2BJ5001 |
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 |