2GQN
Cystathionine Beta-Lyase (CBL) from Escherichia Coli in complex with N-Hydrazinocarbonylmethyl-2-Nitro-Benzamide
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 | 21 |
| Details | BINDING SITE FOR RESIDUE BLP A 700 |
| Chain | Residue |
| A | PHE55 |
| A | ASP185 |
| A | ALA207 |
| A | THR209 |
| A | LYS210 |
| A | MET219 |
| A | TYR338 |
| A | SER339 |
| A | TRP340 |
| A | ARG372 |
| A | HOH873 |
| A | TYR56 |
| A | HOH1134 |
| A | HOH1153 |
| A | ARG58 |
| A | CYS85 |
| A | GLY86 |
| A | ALA87 |
| A | TYR111 |
| A | GLU112 |
| A | GLU154 |
| site_id | AC2 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE BLP B 700 |
| Chain | Residue |
| B | TYR56 |
| B | ARG58 |
| B | CYS85 |
| B | GLY86 |
| B | ALA87 |
| B | TYR111 |
| B | PRO113 |
| B | GLU154 |
| B | ASP185 |
| B | ALA207 |
| B | THR209 |
| B | LYS210 |
| B | MET219 |
| B | TYR238 |
| B | TYR338 |
| B | SER339 |
| B | TRP340 |
| B | ARG372 |
| B | HOH725 |
| B | HOH742 |
| B | HOH870 |
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 | LYS210 | |
| B | LYS210 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| A | TYR111 | |
| A | ASP185 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| B | ARG58 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| B | TYR111 | |
| B | ASP185 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| A | ARG58 |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| A | TYR111 | |
| A | ASP185 | |
| A | LYS210 |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| B | TYR111 | |
| B | ASP185 | |
| B | LYS210 |
| 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 | LYS210 | 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 | LYS210 | covalent catalysis, proton shuttle (general acid/base) |
