4U1T
The crystal structure of holo CalE6, a methionine gamma lyase from Micromonospora echinospora
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0016846 | molecular_function | carbon-sulfur lyase activity |
| A | 0019346 | biological_process | transsulfuration |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0016846 | molecular_function | carbon-sulfur lyase activity |
| B | 0019346 | biological_process | transsulfuration |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0016846 | molecular_function | carbon-sulfur lyase activity |
| C | 0019346 | biological_process | transsulfuration |
| C | 0030170 | molecular_function | pyridoxal phosphate binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0016846 | molecular_function | carbon-sulfur lyase activity |
| D | 0019346 | biological_process | transsulfuration |
| D | 0030170 | molecular_function | pyridoxal phosphate binding |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0016846 | molecular_function | carbon-sulfur lyase activity |
| E | 0019346 | biological_process | transsulfuration |
| E | 0030170 | molecular_function | pyridoxal phosphate binding |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0016846 | molecular_function | carbon-sulfur lyase activity |
| F | 0019346 | biological_process | transsulfuration |
| F | 0030170 | molecular_function | pyridoxal phosphate binding |
| G | 0005737 | cellular_component | cytoplasm |
| G | 0016846 | molecular_function | carbon-sulfur lyase activity |
| G | 0019346 | biological_process | transsulfuration |
| G | 0030170 | molecular_function | pyridoxal phosphate binding |
| H | 0005737 | cellular_component | cytoplasm |
| H | 0016846 | molecular_function | carbon-sulfur lyase activity |
| H | 0019346 | biological_process | transsulfuration |
| H | 0030170 | molecular_function | pyridoxal phosphate binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | binding site for residue SO4 A 401 |
| Chain | Residue |
| A | TYR100 |
| A | HOH787 |
| A | LLP197 |
| A | VAL322 |
| A | SER323 |
| A | THR338 |
| A | ARG358 |
| A | HOH541 |
| A | HOH664 |
| A | HOH754 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | binding site for residue SO4 B 401 |
| Chain | Residue |
| B | TYR100 |
| B | ASN147 |
| B | LLP197 |
| B | SER323 |
| B | THR338 |
| B | ARG358 |
| B | HOH598 |
| B | HOH676 |
| B | HOH758 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 C 401 |
| Chain | Residue |
| C | TYR100 |
| C | LLP197 |
| C | SER323 |
| C | ARG358 |
| C | HOH673 |
| C | HOH686 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 D 401 |
| Chain | Residue |
| D | TYR100 |
| D | LLP197 |
| D | SER323 |
| D | LEU324 |
| D | ARG358 |
| D | HOH699 |
| D | HOH703 |
| site_id | AC5 |
| Number of Residues | 11 |
| Details | binding site for residue SO4 E 401 |
| Chain | Residue |
| E | TYR100 |
| E | ASN147 |
| E | LLP197 |
| E | VAL322 |
| E | SER323 |
| E | LEU324 |
| E | ARG358 |
| E | HOH678 |
| E | HOH680 |
| E | HOH724 |
| E | HOH759 |
| site_id | AC6 |
| Number of Residues | 12 |
| Details | binding site for residue SO4 F 401 |
| Chain | Residue |
| F | TYR100 |
| F | ASN147 |
| F | LLP197 |
| F | VAL322 |
| F | SER323 |
| F | LEU324 |
| F | THR338 |
| F | ARG358 |
| F | HOH635 |
| F | HOH673 |
| F | HOH687 |
| F | HOH759 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 G 401 |
| Chain | Residue |
| G | TYR100 |
| G | LLP197 |
| G | VAL322 |
| G | SER323 |
| G | ARG358 |
| G | HOH597 |
| G | HOH793 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | binding site for residue SO4 H 401 |
| Chain | Residue |
| H | TYR100 |
| H | LLP197 |
| H | VAL322 |
| H | SER323 |
| H | THR338 |
| H | ARG358 |
| H | HOH645 |
| H | HOH769 |
Functional Information from PROSITE/UniProt
| site_id | PS00211 |
| Number of Residues | 15 |
| Details | ABC_TRANSPORTER_1 ABC transporters family signature. FSSGQAAAATLLSLV |
| Chain | Residue | Details |
| A | PHE73-VAL87 |
