2O7C
Crystal structure of L-methionine-lyase from Pseudomonas
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0009086 | biological_process | methionine biosynthetic process |
| 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 | 0003824 | molecular_function | catalytic activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0009086 | biological_process | methionine biosynthetic process |
| 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 | 0003824 | molecular_function | catalytic activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0009086 | biological_process | methionine biosynthetic process |
| 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 | 0003824 | molecular_function | catalytic activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0009086 | biological_process | methionine biosynthetic process |
| 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 | 8 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAY-2003","submissionDatabase":"PDB data bank","title":"Crystal structure of L-methionine alpha-, gamma-lyase.","authors":["Allen T.W.","Sridhar V.","Prasad G.S.","Han Q.","Xu M.","Tan Y.","Hoffman R.M.","Ramaswamy S."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Binding site: {"description":"in other chain","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAY-2003","submissionDatabase":"PDB data bank","title":"Crystal structure of L-methionine alpha-, gamma-lyase.","authors":["Allen T.W.","Sridhar V.","Prasad G.S.","Han Q.","Xu M.","Tan Y.","Hoffman R.M.","Ramaswamy S."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22785484","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3VK3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3VK4","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"17289792","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22785484","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3365412","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAY-2003","submissionDatabase":"PDB data bank","title":"Crystal structure of L-methionine alpha-, gamma-lyase.","authors":["Allen T.W.","Sridhar V.","Prasad G.S.","Han Q.","Xu M.","Tan Y.","Hoffman R.M.","Ramaswamy S."]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"AUG-2003","submissionDatabase":"PDB data bank","title":"Detailed structure of L-methionine-lyase from Pseudomonas putida.","authors":["Misaki S.","Takimoto A.","Takakura T.","Yoshioka T.","Yamashita M.","Tamura T.","Tanaka H.","Inagaki K."]}},{"source":"PDB","id":"1UKJ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
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 |
