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 | 0018315 | biological_process | molybdenum incorporation into molybdenum-molybdopterin complex |
| A | 0032324 | biological_process | molybdopterin cofactor biosynthetic process |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| 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 | 0018315 | biological_process | molybdenum incorporation into molybdenum-molybdopterin complex |
| B | 0032324 | biological_process | molybdopterin cofactor biosynthetic process |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0042803 | molecular_function | protein homodimerization activity |
| 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 |
