5X2Z
Crystal structure of Pseudomonas putida methionine gamma-lyase C116H mutant with L-methionine intermediates
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016846 | molecular_function | carbon-sulfur lyase activity |
| A | 0018826 | molecular_function | methionine gamma-lyase activity |
| A | 0019346 | biological_process | transsulfuration |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0047982 | molecular_function | homocysteine desulfhydrase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016846 | molecular_function | carbon-sulfur lyase activity |
| B | 0018826 | molecular_function | methionine gamma-lyase activity |
| B | 0019346 | biological_process | transsulfuration |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0047982 | molecular_function | homocysteine desulfhydrase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0016829 | molecular_function | lyase activity |
| C | 0016846 | molecular_function | carbon-sulfur lyase activity |
| C | 0018826 | molecular_function | methionine gamma-lyase activity |
| C | 0019346 | biological_process | transsulfuration |
| C | 0030170 | molecular_function | pyridoxal phosphate binding |
| C | 0047982 | molecular_function | homocysteine desulfhydrase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0016829 | molecular_function | lyase activity |
| D | 0016846 | molecular_function | carbon-sulfur lyase activity |
| D | 0018826 | molecular_function | methionine gamma-lyase activity |
| D | 0019346 | biological_process | transsulfuration |
| D | 0030170 | molecular_function | pyridoxal phosphate binding |
| D | 0047982 | molecular_function | homocysteine desulfhydrase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | binding site for residue 3LM A 401 |
| Chain | Residue |
| A | SER88 |
| A | SER340 |
| A | LEU341 |
| A | THR355 |
| A | ARG375 |
| A | HOH510 |
| A | HOH552 |
| A | GLY89 |
| A | MET90 |
| A | TYR114 |
| A | ASP186 |
| A | SER208 |
| A | THR210 |
| A | LYS211 |
| A | VAL339 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | binding site for residue 3LM B 401 |
| Chain | Residue |
| B | SER88 |
| B | GLY89 |
| B | MET90 |
| B | TYR114 |
| B | ASN161 |
| B | ASP186 |
| B | SER208 |
| B | THR210 |
| B | LYS211 |
| B | VAL339 |
| B | SER340 |
| B | LEU341 |
| B | THR355 |
| B | ARG375 |
| B | HOH518 |
| B | HOH552 |
| site_id | AC3 |
| Number of Residues | 15 |
| Details | binding site for residue 3LM C 401 |
| Chain | Residue |
| C | SER88 |
| C | GLY89 |
| C | MET90 |
| C | TYR114 |
| C | ASP186 |
| C | SER208 |
| C | THR210 |
| C | LYS211 |
| C | VAL339 |
| C | SER340 |
| C | LEU341 |
| C | ARG375 |
| C | HOH505 |
| C | HOH549 |
| C | HOH563 |
| site_id | AC4 |
| Number of Residues | 16 |
| Details | binding site for residue 3LM D 401 |
| Chain | Residue |
| D | SER88 |
| D | GLY89 |
| D | MET90 |
| D | TYR114 |
| D | ASN161 |
| D | ASP186 |
| D | SER208 |
| D | THR210 |
| D | LYS211 |
| D | VAL339 |
| D | SER340 |
| D | LEU341 |
| D | THR355 |
| D | ARG375 |
| D | HOH515 |
| D | HOH522 |
Functional Information from PROSITE/UniProt
| site_id | PS00868 |
| Number of Residues | 15 |
| Details | CYS_MET_METAB_PP Cys/Met metabolism enzymes pyridoxal-phosphate attachment site. DLvvhSATKYLsGHG |
| Chain | Residue | Details |
| A | ASP203-GLY217 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|Ref.7 |
| Chain | Residue | Details |
| A | TYR59 | |
| B | TYR59 | |
| C | TYR59 | |
| D | TYR59 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: in other chain => ECO:0000269|Ref.7 |
| Chain | Residue | Details |
| A | GLY89 | |
| A | SER208 | |
| B | GLY89 | |
| B | SER208 | |
| C | GLY89 | |
| C | SER208 | |
| D | GLY89 | |
| D | SER208 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22785484, ECO:0007744|PDB:3VK3, ECO:0007744|PDB:3VK4 |
| Chain | Residue | Details |
| A | TYR114 | |
| A | ARG375 | |
| B | TYR114 | |
| B | ARG375 | |
| C | TYR114 | |
| C | ARG375 | |
| D | TYR114 | |
| D | ARG375 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:17289792, ECO:0000269|PubMed:22785484, ECO:0000269|PubMed:3365412, ECO:0000269|Ref.7, ECO:0000269|Ref.8, ECO:0007744|PDB:1UKJ |
| Chain | Residue | Details |
| A | LYS211 | |
| B | LYS211 | |
| C | LYS211 | |
| D | LYS211 |
