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 | 0004124 | molecular_function | cysteine synthase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0006535 | biological_process | cysteine biosynthetic process from serine |
A | 0016829 | molecular_function | lyase activity |
A | 0019343 | biological_process | cysteine biosynthetic process via cystathionine |
A | 0019344 | biological_process | cysteine biosynthetic process |
A | 0020037 | molecular_function | heme binding |
A | 0030170 | molecular_function | pyridoxal phosphate binding |
A | 0046872 | molecular_function | metal ion binding |
A | 0080146 | molecular_function | L-cysteine desulfhydrase activity |
B | 0004122 | molecular_function | cystathionine beta-synthase activity |
B | 0004124 | molecular_function | cysteine synthase activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0006535 | biological_process | cysteine biosynthetic process from serine |
B | 0016829 | molecular_function | lyase activity |
B | 0019343 | biological_process | cysteine biosynthetic process via cystathionine |
B | 0019344 | biological_process | cysteine biosynthetic process |
B | 0020037 | molecular_function | heme binding |
B | 0030170 | molecular_function | pyridoxal phosphate binding |
B | 0046872 | molecular_function | metal ion binding |
B | 0080146 | molecular_function | L-cysteine desulfhydrase activity |
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 | 4 |
Details | BINDING: axial binding residue => ECO:0000269|PubMed:29275181 |
Chain | Residue | Details |
A | CYS12 | |
A | HIS23 | |
B | CYS12 | |
B | HIS23 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:29275181 |
Chain | Residue | Details |
B | GLY215 | |
B | SER307 | |
A | GLY215 | |
A | SER307 | |
B | ASN108 | |
A | ASN108 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:29275181 |
Chain | Residue | Details |
A | LYS78 | |
B | LYS78 |