2O7C
Crystal structure of L-methionine-lyase from Pseudomonas
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 | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 400 |
| Chain | Residue |
| A | TYR114 |
| A | VAL339 |
| A | SER340 |
| A | GLN349 |
| A | ARG375 |
| A | HOH503 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 900 |
| Chain | Residue |
| B | ARG875 |
| B | HOH931 |
| B | HOH1068 |
| B | TYR614 |
| B | SER840 |
| B | GLN849 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 C 1400 |
| Chain | Residue |
| C | TYR1114 |
| C | VAL1339 |
| C | SER1340 |
| C | GLN1349 |
| C | ARG1375 |
| C | HOH1406 |
| C | HOH1411 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 D 1900 |
| Chain | Residue |
| D | TYR1614 |
| D | LLP1711 |
| D | VAL1839 |
| D | SER1840 |
| D | GLN1849 |
| D | ARG1875 |
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 | TYR559 | |
| C | TYR1059 | |
| D | TYR1559 |
| 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 | GLY589 | |
| B | SER708 | |
| C | GLY1089 | |
| C | SER1208 | |
| D | GLY1589 | |
| D | SER1708 |
| 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 | TYR614 | |
| B | ARG875 | |
| C | TYR1114 | |
| C | ARG1375 | |
| D | TYR1614 | |
| D | ARG1875 |
| 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 | LLP711 | |
| C | LLP1211 | |
| D | LLP1711 |
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 | ASP686 | |
| B | TYR614 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| C | TYR1114 | |
| C | ASP1186 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| D | TYR1614 | |
| D | ASP1686 |
| site_id | CSA5 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| A | ARG61 |
| site_id | CSA6 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| B | ARG561 |
| site_id | CSA7 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| C | ARG1061 |
| site_id | CSA8 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| D | ARG1561 |
