1CL1
CYSTATHIONINE BETA-LYASE (CBL) FROM ESCHERICHIA COLI
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006520 | biological_process | amino acid metabolic process |
| A | 0008784 | molecular_function | alanine racemase activity |
| A | 0009086 | biological_process | methionine biosynthetic process |
| A | 0016829 | molecular_function | lyase activity |
| A | 0019346 | biological_process | transsulfuration |
| A | 0019450 | biological_process | L-cysteine catabolic process to pyruvate |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0032991 | cellular_component | protein-containing complex |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0047804 | molecular_function | cysteine-S-conjugate beta-lyase activity |
| A | 0051289 | biological_process | protein homotetramerization |
| A | 0080146 | molecular_function | L-cysteine desulfhydrase activity |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006520 | biological_process | amino acid metabolic process |
| B | 0008784 | molecular_function | alanine racemase activity |
| B | 0009086 | biological_process | methionine biosynthetic process |
| B | 0016829 | molecular_function | lyase activity |
| B | 0019346 | biological_process | transsulfuration |
| B | 0019450 | biological_process | L-cysteine catabolic process to pyruvate |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0032991 | cellular_component | protein-containing complex |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0047804 | molecular_function | cysteine-S-conjugate beta-lyase activity |
| B | 0051289 | biological_process | protein homotetramerization |
| B | 0080146 | molecular_function | L-cysteine desulfhydrase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE BCT A 402 |
| Chain | Residue |
| A | TYR111 |
| A | LLP210 |
| A | SER339 |
| A | TRP340 |
| A | ARG372 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE BCT B 403 |
| Chain | Residue |
| B | SER339 |
| B | TRP340 |
| B | ARG372 |
| B | TYR111 |
| B | LLP210 |
| site_id | PLA |
| Number of Residues | 1 |
| Details | BINDING SITE |
| Chain | Residue |
| A | LLP210 |
| site_id | PLB |
| Number of Residues | 1 |
| Details | BINDING SITE |
| Chain | Residue |
| B | LLP210 |
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. DVsiqAATKYLvGHS |
| Chain | Residue | Details |
| A | ASP202-SER216 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:3307782, ECO:0000269|PubMed:8831789 |
| Chain | Residue | Details |
| A | LLP210 | |
| B | LLP210 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | a catalytic site defined by CSA, PubMed 8831789 |
| Chain | Residue | Details |
| A | TYR111 |
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 449 |
| Chain | Residue | Details |
| A | ARG58 | increase nucleophilicity |
| A | TYR111 | electrostatic stabiliser, proton shuttle (general acid/base) |
| A | ASP185 | electrostatic stabiliser |
| A | LLP210 | covalent catalysis, proton shuttle (general acid/base) |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 449 |
| Chain | Residue | Details |
| B | ARG58 | increase nucleophilicity |
| B | TYR111 | electrostatic stabiliser, proton shuttle (general acid/base) |
| B | ASP185 | electrostatic stabiliser |
| B | LLP210 | covalent catalysis, proton shuttle (general acid/base) |
