5OHX
Structure of active cystathionine B-synthase from Apis mellifera
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004122 | molecular_function | cystathionine beta-synthase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006535 | biological_process | L-cysteine biosynthetic process from L-serine |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0016829 | molecular_function | lyase activity |
| A | 0019343 | biological_process | L-cysteine biosynthetic process via L-cystathionine |
| A | 0019344 | biological_process | L-cysteine biosynthetic process |
| A | 0020037 | molecular_function | heme binding |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0004122 | molecular_function | cystathionine beta-synthase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006535 | biological_process | L-cysteine biosynthetic process from L-serine |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0016829 | molecular_function | lyase activity |
| B | 0019343 | biological_process | L-cysteine biosynthetic process via L-cystathionine |
| B | 0019344 | biological_process | L-cysteine biosynthetic process |
| B | 0020037 | molecular_function | heme binding |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | binding site for residue HEM A 701 |
| Chain | Residue |
| A | ARG8 |
| A | HIS23 |
| A | PRO185 |
| A | PRO188 |
| A | TYR192 |
| A | ARG225 |
| A | VAL272 |
| A | SER10 |
| A | TYR11 |
| A | CYS12 |
| A | THR13 |
| A | TRP14 |
| A | ALA18 |
| A | ASN20 |
| A | SER21 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | binding site for residue PLP A 702 |
| Chain | Residue |
| A | LYS78 |
| A | ASN108 |
| A | GLY213 |
| A | ALA214 |
| A | GLY215 |
| A | THR216 |
| A | GLY217 |
| A | GLY218 |
| A | THR219 |
| A | GLY263 |
| A | SER307 |
| A | PRO333 |
| A | ASP334 |
| site_id | AC3 |
| Number of Residues | 17 |
| Details | binding site for residue HEM B 701 |
| Chain | Residue |
| B | ARG8 |
| B | SER10 |
| B | TYR11 |
| B | CYS12 |
| B | THR13 |
| B | TRP14 |
| B | ALA18 |
| B | ASN20 |
| B | SER21 |
| B | PRO22 |
| B | HIS23 |
| B | PRO185 |
| B | PRO188 |
| B | TYR192 |
| B | ARG225 |
| B | VAL272 |
| B | HIS475 |
| site_id | AC4 |
| Number of Residues | 13 |
| Details | binding site for residue PLP B 702 |
| Chain | Residue |
| B | LYS78 |
| B | ASN108 |
| B | ALA214 |
| B | GLY215 |
| B | THR216 |
| B | GLY217 |
| B | GLY218 |
| B | THR219 |
| B | GLY263 |
| B | ILE264 |
| B | SER307 |
| B | PRO333 |
| B | ASP334 |
Functional Information from PROSITE/UniProt
| site_id | PS00901 |
| Number of Residues | 19 |
| Details | CYS_SYNTHASE Cysteine synthase/cystathionine beta-synthase P-phosphate attachment site. KcEfln.PGgSVKdRiAyrM |
| Chain | Residue | Details |
| A | LYS67-MET85 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 118 |
| Details | Domain: {"description":"CBS 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00703","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"29275181","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"29275181","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"29275181","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
