1V7U
Crystal structure of Undecaprenyl Pyrophosphate Synthase with farnesyl pyrophosphate
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0004659 | molecular_function | prenyltransferase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0008360 | biological_process | regulation of cell shape |
A | 0008834 | molecular_function | ditrans,polycis-undecaprenyl-diphosphate synthase [(2E,6E)-farnesyl-diphosphate specific] 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 | ditrans,polycis-polyprenyl diphosphate synthase [(2E,6E)-farnesyl diphosphate specific] 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 | 0004659 | molecular_function | prenyltransferase activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0008360 | biological_process | regulation of cell shape |
B | 0008834 | molecular_function | ditrans,polycis-undecaprenyl-diphosphate synthase [(2E,6E)-farnesyl-diphosphate specific] 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 | ditrans,polycis-polyprenyl diphosphate synthase [(2E,6E)-farnesyl diphosphate specific] 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 | 13 |
Details | BINDING SITE FOR RESIDUE FPP A 501 |
Chain | Residue |
A | ASP26 |
A | GLU81 |
A | LEU85 |
A | LEU88 |
A | TRP221 |
A | GLY27 |
A | ASN28 |
A | GLY29 |
A | ARG30 |
A | ARG39 |
A | HIS43 |
A | VAL50 |
A | ALA69 |
site_id | AC2 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE FPP A 502 |
Chain | Residue |
A | ARG51 |
A | SER55 |
A | PHE89 |
A | ALA92 |
A | LEU93 |
A | SER99 |
A | LEU100 |
A | HIS103 |
A | HOH516 |
A | HOH556 |
B | ASN166 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE FPP B 503 |
Chain | Residue |
B | PHE89 |
B | LEU93 |
B | GLU96 |
B | HOH750 |
Functional Information from PROSITE/UniProt
site_id | PS01066 |
Number of Residues | 18 |
Details | UPP_SYNTHASE Undecaprenyl pyrophosphate synthase family signature. DLVIRTGGehRiSnFLLW |
Chain | Residue | Details |
A | ASP190-TRP207 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | Active site: {} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | Active site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 18 |
Details | Binding site: {} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 3 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"15044730","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 7 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"15044730","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | Site: {"description":"Required for continued chain elongation"} |
Chain | Residue | Details |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | Site: {"description":"Important for determining product length"} |
Chain | Residue | Details |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1f75 |
Chain | Residue | Details |
A | ARG30 | |
A | ARG200 | |
A | ARG39 | |
A | ARG194 |
site_id | CSA2 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1f75 |
Chain | Residue | Details |
B | ARG30 | |
B | ARG200 | |
B | ARG39 | |
B | ARG194 |