3FGP
2.05 a Crystal Structure of CysM from Mycobacterium Tuberculosis - Open and Closed Conformations
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004124 | molecular_function | cysteine synthase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006535 | biological_process | cysteine biosynthetic process from serine |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016765 | molecular_function | transferase activity, transferring alkyl or aryl (other than methyl) groups |
| A | 0019344 | biological_process | cysteine biosynthetic process |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0032991 | cellular_component | protein-containing complex |
| A | 0033847 | molecular_function | O-phosphoserine sulfhydrylase activity |
| B | 0004124 | molecular_function | cysteine synthase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006535 | biological_process | cysteine biosynthetic process from serine |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016765 | molecular_function | transferase activity, transferring alkyl or aryl (other than methyl) groups |
| B | 0019344 | biological_process | cysteine biosynthetic process |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0032991 | cellular_component | protein-containing complex |
| B | 0033847 | molecular_function | O-phosphoserine sulfhydrylase activity |
Functional Information from PROSITE/UniProt
| site_id | PS00901 |
| Number of Residues | 19 |
| Details | CYS_SYNTHASE Cysteine synthase/cystathionine beta-synthase P-phosphate attachment site. KlEdrn.PTgSIKdRpAvrM |
| Chain | Residue | Details |
| A | LYS40-MET58 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:18771296, ECO:0000269|PubMed:18799456, ECO:0000269|PubMed:19101553 |
| Chain | Residue | Details |
| A | ASN81 | |
| A | SER265 | |
| B | ASN81 | |
| B | SER265 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | GLY184 | |
| B | GLY184 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000305 |
| Chain | Residue | Details |
| A | ARG220 | |
| B | ARG220 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine |
| Chain | Residue | Details |
| A | LLP51 | |
| B | LLP51 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1oas |
| Chain | Residue | Details |
| A | SER265 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1oas |
| Chain | Residue | Details |
| B | SER265 |
