1G8L
CRYSTAL STRUCTURE OF ESCHERICHIA COLI MOEA
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005515 | molecular_function | protein binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0006777 | biological_process | Mo-molybdopterin cofactor biosynthetic process |
A | 0016740 | molecular_function | transferase activity |
A | 0032324 | biological_process | molybdopterin cofactor biosynthetic process |
A | 0042802 | molecular_function | identical protein binding |
A | 0042803 | molecular_function | protein homodimerization activity |
A | 0046872 | molecular_function | metal ion binding |
A | 0061599 | molecular_function | molybdopterin molybdotransferase activity |
B | 0005515 | molecular_function | protein binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0006777 | biological_process | Mo-molybdopterin cofactor biosynthetic process |
B | 0016740 | molecular_function | transferase activity |
B | 0032324 | biological_process | molybdopterin cofactor biosynthetic process |
B | 0042802 | molecular_function | identical protein binding |
B | 0042803 | molecular_function | protein homodimerization activity |
B | 0046872 | molecular_function | metal ion binding |
B | 0061599 | molecular_function | molybdopterin molybdotransferase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL A 701 |
Chain | Residue |
A | PHE374 |
A | SER375 |
A | SER378 |
A | HOH765 |
A | HOH865 |
A | HOH934 |
B | ILE143 |
B | PHE150 |
B | VAL163 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL B 702 |
Chain | Residue |
A | THR157 |
A | GLU160 |
A | HOH855 |
B | SER378 |
B | GLY380 |
B | PHE408 |
B | HOH829 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL B 703 |
Chain | Residue |
A | ILE143 |
A | VAL163 |
B | PHE374 |
B | SER375 |
B | HOH837 |
B | HOH864 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 704 |
Chain | Residue |
A | SER378 |
A | PHE408 |
A | HOH723 |
A | HOH866 |
B | GLU160 |
B | HOH800 |
site_id | AC5 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL B 705 |
Chain | Residue |
B | GLY37 |
B | ILE39 |
B | LYS177 |
B | VAL178 |
B | LEU216 |
B | GLY217 |
B | HOH721 |
B | HOH724 |
site_id | AC6 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL A 706 |
Chain | Residue |
A | GLY37 |
A | ARG176 |
A | LYS177 |
A | VAL178 |
A | GLY217 |
A | SER320 |
A | HOH755 |
A | HOH881 |
site_id | AC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL B 707 |
Chain | Residue |
B | GLU188 |
B | ASP228 |
B | GLY252 |
B | SER254 |
B | ASP259 |
B | HOH802 |
B | HOH862 |
site_id | AC8 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL B 708 |
Chain | Residue |
B | GLY186 |
B | ASP187 |
B | LEU189 |
B | ILE225 |
B | ARG227 |
B | HOH812 |
B | HOH823 |
site_id | AC9 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 709 |
Chain | Residue |
A | PRO230 |
A | HIS231 |
A | GOL717 |
A | HOH774 |
B | ARG179 |
B | GLU219 |
B | ILE221 |
site_id | BC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL B 710 |
Chain | Residue |
B | VAL255 |
B | PRO283 |
B | PRO298 |
B | GLY299 |
B | HOH845 |
B | HOH920 |
site_id | BC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL B 711 |
Chain | Residue |
B | GLY281 |
B | ARG345 |
B | HOH848 |
site_id | BC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL B 712 |
Chain | Residue |
A | ALA145 |
A | HOH883 |
B | GLU387 |
B | ARG390 |
site_id | BC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL B 713 |
Chain | Residue |
B | LEU10 |
B | ASP11 |
B | ARG330 |
B | LEU346 |
site_id | BC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL A 714 |
Chain | Residue |
A | SER19 |
A | VAL21 |
A | THR22 |
A | LYS318 |
site_id | BC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL A 715 |
Chain | Residue |
A | LYS79 |
A | GLN84 |
A | PRO85 |
A | TYR86 |
A | HIS87 |
site_id | BC7 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL B 716 |
Chain | Residue |
B | ARG176 |
B | ARG179 |
B | ASP241 |
B | SER242 |
B | GLN243 |
B | ALA244 |
B | ASP245 |
B | ASN291 |
site_id | BC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL A 717 |
Chain | Residue |
A | ASP228 |
A | ASP229 |
A | PRO230 |
A | GOL709 |
site_id | BC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL B 718 |
Chain | Residue |
B | THR364 |
B | THR365 |
B | GLY367 |
Functional Information from PROSITE/UniProt
site_id | PS01079 |
Number of Residues | 34 |
Details | MOCF_BIOSYNTHESIS_2 Molybdenum cofactor biosynthesis proteins signature 2. SvGeaDytktiLeelgeiafwk..LaiKPGKPfaFG |
Chain | Residue | Details |
A | SER254-GLY287 |