1IBJ
Crystal structure of cystathionine beta-lyase from Arabidopsis thaliana
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006555 | biological_process | methionine metabolic process |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0009086 | biological_process | methionine biosynthetic process |
| A | 0009507 | cellular_component | chloroplast |
| A | 0009570 | cellular_component | chloroplast stroma |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016846 | molecular_function | carbon-sulfur lyase activity |
| A | 0019279 | biological_process | L-methionine biosynthetic process from L-homoserine via cystathionine |
| A | 0019346 | biological_process | transsulfuration |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0047804 | molecular_function | cysteine-S-conjugate beta-lyase activity |
| A | 0060090 | molecular_function | molecular adaptor activity |
| A | 0071266 | biological_process | 'de novo' L-methionine biosynthetic process |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006555 | biological_process | methionine metabolic process |
| C | 0008652 | biological_process | amino acid biosynthetic process |
| C | 0009086 | biological_process | methionine biosynthetic process |
| C | 0009507 | cellular_component | chloroplast |
| C | 0009570 | cellular_component | chloroplast stroma |
| C | 0016829 | molecular_function | lyase activity |
| C | 0016846 | molecular_function | carbon-sulfur lyase activity |
| C | 0019279 | biological_process | L-methionine biosynthetic process from L-homoserine via cystathionine |
| C | 0019346 | biological_process | transsulfuration |
| C | 0030170 | molecular_function | pyridoxal phosphate binding |
| C | 0042803 | molecular_function | protein homodimerization activity |
| C | 0047804 | molecular_function | cysteine-S-conjugate beta-lyase activity |
| C | 0060090 | molecular_function | molecular adaptor activity |
| C | 0071266 | biological_process | 'de novo' L-methionine biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CO3 A 1401 |
| Chain | Residue |
| A | TYR181 |
| A | SER405 |
| A | ARG440 |
| A | PLP1400 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CO3 C 2401 |
| Chain | Residue |
| C | HOH2463 |
| C | LYS278 |
| C | SER405 |
| C | PHE406 |
| C | ARG440 |
| C | PLP2400 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SO4 A 500 |
| Chain | Residue |
| A | GLY365 |
| A | HIS366 |
| A | HIS367 |
| A | LEU368 |
| C | HIS363 |
| C | PRO364 |
| C | GLY365 |
| C | HIS366 |
| C | HIS367 |
| C | LEU368 |
| site_id | AC4 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE PLP A 1400 |
| Chain | Residue |
| A | SER156 |
| A | GLY157 |
| A | MET158 |
| A | TYR181 |
| A | GLU224 |
| A | ASP253 |
| A | SER275 |
| A | THR277 |
| A | LYS278 |
| A | MET287 |
| A | PHE406 |
| A | CO31401 |
| A | HOH1522 |
| C | TYR127 |
| C | ARG129 |
| site_id | AC5 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE PLP C 2400 |
| Chain | Residue |
| A | TYR127 |
| A | ARG129 |
| C | GLY157 |
| C | MET158 |
| C | TYR181 |
| C | GLU224 |
| C | ASP253 |
| C | SER275 |
| C | THR277 |
| C | LYS278 |
| C | MET287 |
| C | ALA288 |
| C | PHE406 |
| C | CO32401 |
| C | HOH2463 |
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. DIvmhSATKFIaGHS |
| Chain | Residue | Details |
| A | ASP270-SER284 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11402193","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1IBJ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"11402193","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1IBJ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| A | TYR181 | |
| A | LYS278 | |
| A | ASP253 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| C | TYR181 | |
| C | LYS278 | |
| C | ASP253 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| A | ARG129 | |
| C | TYR181 | |
| C | ASP253 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| A | TYR181 | |
| A | ASP253 | |
| C | ARG129 |
