4GR5
Crystal structure of SlgN1deltaAsub in complex with AMPcPP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0008168 | molecular_function | methyltransferase activity |
| A | 0031177 | molecular_function | phosphopantetheine binding |
| A | 0043041 | biological_process | amino acid activation for nonribosomal peptide biosynthetic process |
| A | 0044550 | biological_process | secondary metabolite biosynthetic process |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0008168 | molecular_function | methyltransferase activity |
| B | 0031177 | molecular_function | phosphopantetheine binding |
| B | 0043041 | biological_process | amino acid activation for nonribosomal peptide biosynthetic process |
| B | 0044550 | biological_process | secondary metabolite biosynthetic process |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| C | 0008168 | molecular_function | methyltransferase activity |
| C | 0031177 | molecular_function | phosphopantetheine binding |
| C | 0043041 | biological_process | amino acid activation for nonribosomal peptide biosynthetic process |
| C | 0044550 | biological_process | secondary metabolite biosynthetic process |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005829 | cellular_component | cytosol |
| D | 0008168 | molecular_function | methyltransferase activity |
| D | 0031177 | molecular_function | phosphopantetheine binding |
| D | 0043041 | biological_process | amino acid activation for nonribosomal peptide biosynthetic process |
| D | 0044550 | biological_process | secondary metabolite biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE APC A 601 |
| Chain | Residue |
| A | LYS227 |
| A | PRO358 |
| A | ALA359 |
| A | GLU360 |
| A | ASP449 |
| A | TYR461 |
| A | ARG464 |
| A | HOH701 |
| A | HOH702 |
| A | HOH703 |
| A | HOH723 |
| A | TRP262 |
| A | HOH789 |
| A | HOH829 |
| A | HOH844 |
| A | HOH890 |
| A | HOH893 |
| A | HOH923 |
| A | GLY332 |
| A | GLU333 |
| A | PRO334 |
| A | ASN354 |
| A | GLY355 |
| A | TYR356 |
| A | GLY357 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE TLA A 602 |
| Chain | Residue |
| A | ARG21 |
| A | ARG234 |
| A | GLY413 |
| A | ALA414 |
| A | LEU416 |
| A | ARG443 |
| A | HOH716 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 603 |
| Chain | Residue |
| A | PRO86 |
| A | ASP87 |
| A | HOH1006 |
| site_id | AC4 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE APC B 601 |
| Chain | Residue |
| B | LYS227 |
| B | TRP262 |
| B | GLY332 |
| B | GLU333 |
| B | PRO334 |
| B | ASN354 |
| B | GLY355 |
| B | TYR356 |
| B | GLY357 |
| B | PRO358 |
| B | ALA359 |
| B | GLU360 |
| B | ASP449 |
| B | TYR461 |
| B | ARG464 |
| B | HOH701 |
| B | HOH702 |
| B | HOH703 |
| B | HOH738 |
| B | HOH791 |
| B | HOH817 |
| B | HOH880 |
| B | HOH882 |
| B | HOH903 |
| B | HOH910 |
| B | HOH919 |
| B | HOH933 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE TLA B 602 |
| Chain | Residue |
| B | GLU52 |
| B | ARG225 |
| B | SER422 |
| B | ARG423 |
| B | PRO424 |
| B | ALA425 |
| B | LEU426 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE TLA B 603 |
| Chain | Residue |
| B | ARG21 |
| B | ARG234 |
| B | GLY413 |
| B | ALA414 |
| B | GLU442 |
| B | ARG443 |
| B | HOH735 |
| site_id | AC7 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE APC C 601 |
| Chain | Residue |
| C | LYS227 |
| C | TRP262 |
| C | GLY332 |
| C | GLU333 |
| C | PRO334 |
| C | ASN354 |
| C | GLY355 |
| C | TYR356 |
| C | GLY357 |
| C | PRO358 |
| C | ALA359 |
| C | GLU360 |
| C | ASP449 |
| C | TYR461 |
| C | ARG464 |
| C | HOH706 |
| C | HOH707 |
| C | HOH708 |
| C | HOH752 |
| C | HOH773 |
| C | HOH828 |
| C | HOH829 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE TLA C 602 |
| Chain | Residue |
| C | ARG234 |
| C | GLY413 |
| C | ALA414 |
| C | GLU442 |
| C | ARG443 |
| C | HOH836 |
| C | ARG21 |
| site_id | AC9 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE APC D 601 |
| Chain | Residue |
| D | LYS227 |
| D | TRP262 |
| D | GLY332 |
| D | GLU333 |
| D | PRO334 |
| D | ASN354 |
| D | GLY355 |
| D | TYR356 |
| D | GLY357 |
| D | PRO358 |
| D | ALA359 |
| D | GLU360 |
| D | ASP449 |
| D | TYR461 |
| D | ARG464 |
| D | HOH1032 |
| D | HOH1036 |
| D | HOH1037 |
| D | HOH1038 |
| D | HOH1054 |
| D | HOH1116 |
| D | HOH1120 |
| D | HOH1127 |
| D | HOH1241 |
| D | HOH1262 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE TLA D 602 |
| Chain | Residue |
| D | GLU52 |
| D | ARG225 |
| D | ARG423 |
| D | PRO424 |
| D | ALA425 |
| D | LEU426 |
| site_id | BC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE TLA D 603 |
| Chain | Residue |
| D | ARG21 |
| D | ARG234 |
| D | GLY413 |
| D | ALA414 |
| D | GLU442 |
| D | ARG443 |
| D | HOH1125 |
Functional Information from PROSITE/UniProt
| site_id | PS00455 |
| Number of Residues | 12 |
| Details | AMP_BINDING Putative AMP-binding domain signature. VMFTSGSTGrPK |
| Chain | Residue | Details |
| A | VAL216-LYS227 |
| site_id | PS00840 |
| Number of Residues | 34 |
| Details | SUMT_2 Uroporphyrin-III C-methyltransferase signature 2. ValLheADeltYGalneranrLahrlvgLgVaPG |
| Chain | Residue | Details |
| A | VAL89-GLY122 |
