1GC2
CRYSTAL STRUCTURE OF THE PYRIDOXAL-5'-PHOSPHATE DEPENDENT L-METHIONINE GAMMA-LYASE FROM PSEUDOMONAS PUTIDA
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 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 | LLP211 | |
| B | LLP211 | |
| C | LLP211 | |
| D | LLP211 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| A | ASP186 | |
| A | TYR114 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| B | ASP186 | |
| B | TYR114 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| C | ASP186 | |
| C | TYR114 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| D | ASP186 | |
| D | TYR114 |
