4ITX
P113S mutant of E. coli Cystathionine beta-lyase MetC inhibited by reaction with L-Ala-P
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006520 | biological_process | amino acid metabolic process |
| A | 0008652 | biological_process | amino acid biosynthetic 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 | 0005737 | cellular_component | cytoplasm |
| B | 0006520 | biological_process | amino acid metabolic process |
| B | 0008652 | biological_process | amino acid biosynthetic 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 | 20 |
| Details | BINDING SITE FOR RESIDUE IN5 A 401 |
| Chain | Residue |
| A | TYR56 |
| A | THR209 |
| A | LYS210 |
| A | MET219 |
| A | TYR338 |
| A | SER339 |
| A | TRP340 |
| A | ARG372 |
| A | HOH524 |
| A | HOH551 |
| A | HOH619 |
| A | ARG58 |
| A | HOH632 |
| A | CYS85 |
| A | GLY86 |
| A | ALA87 |
| A | TYR111 |
| A | GLU154 |
| A | ASP185 |
| A | ALA207 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA A 402 |
| Chain | Residue |
| A | ASN12 |
| A | HOH575 |
| A | HOH606 |
| A | HOH674 |
| B | LEU333 |
| B | GLU344 |
| B | HOH730 |
| site_id | AC3 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE IN5 B 401 |
| Chain | Residue |
| B | TYR56 |
| B | ARG58 |
| B | CYS85 |
| B | GLY86 |
| B | ALA87 |
| B | TYR111 |
| B | GLU154 |
| B | ASP185 |
| B | ALA207 |
| B | THR209 |
| B | LYS210 |
| B | MET219 |
| B | TYR338 |
| B | SER339 |
| B | TRP340 |
| B | ARG372 |
| B | HOH519 |
| B | HOH557 |
| B | HOH567 |
| B | HOH610 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA B 402 |
| Chain | Residue |
| A | LEU333 |
| A | GLU344 |
| B | ASN12 |
| B | HOH546 |
| B | HOH656 |
| B | HOH675 |
| B | HOH676 |
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 | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"3307782","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8831789","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
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 | 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) |
