1N1D
Glycerol-3-phosphate cytidylyltransferase complexed with CDP-glycerol
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0009058 | biological_process | biosynthetic process |
A | 0016779 | molecular_function | nucleotidyltransferase activity |
A | 0019350 | biological_process | teichoic acid biosynthetic process |
A | 0046872 | molecular_function | metal ion binding |
A | 0047348 | molecular_function | glycerol-3-phosphate cytidylyltransferase activity |
A | 0071555 | biological_process | cell wall organization |
B | 0003824 | molecular_function | catalytic activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0009058 | biological_process | biosynthetic process |
B | 0016779 | molecular_function | nucleotidyltransferase activity |
B | 0019350 | biological_process | teichoic acid biosynthetic process |
B | 0046872 | molecular_function | metal ion binding |
B | 0047348 | molecular_function | glycerol-3-phosphate cytidylyltransferase activity |
B | 0071555 | biological_process | cell wall organization |
C | 0003824 | molecular_function | catalytic activity |
C | 0005737 | cellular_component | cytoplasm |
C | 0009058 | biological_process | biosynthetic process |
C | 0016779 | molecular_function | nucleotidyltransferase activity |
C | 0019350 | biological_process | teichoic acid biosynthetic process |
C | 0046872 | molecular_function | metal ion binding |
C | 0047348 | molecular_function | glycerol-3-phosphate cytidylyltransferase activity |
C | 0071555 | biological_process | cell wall organization |
D | 0003824 | molecular_function | catalytic activity |
D | 0005737 | cellular_component | cytoplasm |
D | 0009058 | biological_process | biosynthetic process |
D | 0016779 | molecular_function | nucleotidyltransferase activity |
D | 0019350 | biological_process | teichoic acid biosynthetic process |
D | 0046872 | molecular_function | metal ion binding |
D | 0047348 | molecular_function | glycerol-3-phosphate cytidylyltransferase activity |
D | 0071555 | biological_process | cell wall organization |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 A 701 |
Chain | Residue |
A | HIS14 |
A | HIS17 |
A | ARG113 |
A | SER118 |
A | THR119 |
A | C2G130 |
A | HOH909 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 D 702 |
Chain | Residue |
D | THR119 |
D | THR120 |
D | C2G430 |
D | HOH820 |
D | HOH881 |
D | ARG113 |
D | SER118 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 B 705 |
Chain | Residue |
B | HIS14 |
B | HIS17 |
B | SER118 |
B | THR119 |
B | C2G230 |
B | HOH780 |
site_id | AC4 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE C2G A 130 |
Chain | Residue |
A | GLY8 |
A | THR9 |
A | PHE10 |
A | HIS17 |
A | SER36 |
A | LYS44 |
A | LYS46 |
A | GLU71 |
A | LYS77 |
A | MET91 |
A | GLY92 |
A | ASP94 |
A | TRP95 |
A | ARG113 |
A | THR114 |
A | ILE117 |
A | SO4701 |
A | HOH721 |
A | HOH733 |
A | HOH745 |
A | HOH845 |
site_id | AC5 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE C2G B 230 |
Chain | Residue |
B | GLY8 |
B | THR9 |
B | PHE10 |
B | SER36 |
B | LYS44 |
B | LYS46 |
B | GLU71 |
B | TRP74 |
B | LYS77 |
B | GLY92 |
B | ASP94 |
B | TRP95 |
B | PHE99 |
B | ARG113 |
B | THR114 |
B | ILE117 |
B | SO4705 |
B | HOH707 |
B | HOH740 |
B | HOH748 |
B | HOH780 |
site_id | AC6 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE C2G C 330 |
Chain | Residue |
C | TYR7 |
C | GLY8 |
C | THR9 |
C | PHE10 |
C | HIS17 |
C | SER36 |
C | LYS44 |
C | LYS46 |
C | GLU71 |
C | LYS77 |
C | MET91 |
C | GLY92 |
C | ASP94 |
C | TRP95 |
C | ARG113 |
C | THR114 |
C | ILE117 |
C | HOH710 |
C | HOH760 |
C | HOH839 |
site_id | AC7 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE C2G D 430 |
Chain | Residue |
D | HOH723 |
D | HOH739 |
D | HOH812 |
D | HOH820 |
D | HOH892 |
D | GLY8 |
D | THR9 |
D | PHE10 |
D | SER36 |
D | LYS44 |
D | LYS46 |
D | GLU71 |
D | LYS77 |
D | MET91 |
D | GLY92 |
D | ASP94 |
D | TRP95 |
D | ARG113 |
D | THR114 |
D | ILE117 |
D | SO4702 |
D | HOH722 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10508782, ECO:0000269|PubMed:14506262 |
Chain | Residue | Details |
A | THR9 | |
C | HIS14 | |
C | LYS46 | |
C | ARG113 | |
D | THR9 | |
D | HIS14 | |
D | LYS46 | |
D | ARG113 | |
A | HIS14 | |
A | LYS46 | |
A | ARG113 | |
B | THR9 | |
B | HIS14 | |
B | LYS46 | |
B | ARG113 | |
C | THR9 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:14506262 |
Chain | Residue | Details |
A | LYS44 | |
A | LYS77 | |
B | LYS44 | |
B | LYS77 | |
C | LYS44 | |
C | LYS77 | |
D | LYS44 | |
D | LYS77 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 2 |
Details | M-CSA 296 |
Chain | Residue | Details |
A | LYS44 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor |
A | LYS46 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor |
site_id | MCSA2 |
Number of Residues | 2 |
Details | M-CSA 296 |
Chain | Residue | Details |
B | LYS44 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor |
B | LYS46 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor |
site_id | MCSA3 |
Number of Residues | 2 |
Details | M-CSA 296 |
Chain | Residue | Details |
C | LYS44 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor |
C | LYS46 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor |
site_id | MCSA4 |
Number of Residues | 2 |
Details | M-CSA 296 |
Chain | Residue | Details |
D | LYS44 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor |
D | LYS46 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor |