4ITG
P113S mutant of E. coli Cystathionine beta-lyase MetC
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 | 10 |
Details | BINDING SITE FOR RESIDUE EPE A 401 |
Chain | Residue |
A | TYR111 |
A | HOH634 |
A | SER113 |
A | ASP116 |
A | LLP210 |
A | TYR338 |
A | SER339 |
A | TRP340 |
A | ARG372 |
A | HOH624 |
site_id | AC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EPE B 401 |
Chain | Residue |
B | TYR111 |
B | SER113 |
B | ASP116 |
B | LLP210 |
B | TYR338 |
B | SER339 |
B | TRP340 |
B | ARG372 |
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 | 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) |