1D6S
CRYSTAL STRUCTURE OF THE K41A MUTANT OF O-ACETYLSERINE SULFHYDRYLASE COMPLEXED IN EXTERNAL ALDIMINE LINKAGE WITH METHIONINE
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004124 | molecular_function | cysteine synthase activity |
A | 0005737 | cellular_component | cytoplasm |
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 | 0080146 | molecular_function | L-cysteine desulfhydrase activity |
B | 0004124 | molecular_function | cysteine synthase activity |
B | 0005737 | cellular_component | cytoplasm |
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 | 0080146 | molecular_function | L-cysteine desulfhydrase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE MET A 401 |
Chain | Residue |
A | THR68 |
A | ASN69 |
A | GLY70 |
A | ASN71 |
A | THR72 |
A | GLN142 |
A | GLY228 |
A | PLP501 |
site_id | AC2 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE PLP A 501 |
Chain | Residue |
A | ASN71 |
A | GLY176 |
A | THR177 |
A | GLY178 |
A | GLY179 |
A | THR180 |
A | GLY228 |
A | ILE229 |
A | SER272 |
A | PRO299 |
A | SER300 |
A | TYR305 |
A | MET401 |
A | HOH508 |
A | HOH579 |
A | ASN69 |
site_id | AC3 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE PLP B 502 |
Chain | Residue |
B | ASN69 |
B | ASN71 |
B | GLY174 |
B | GLY176 |
B | THR177 |
B | GLY178 |
B | THR180 |
B | GLN227 |
B | GLY228 |
B | ILE229 |
B | SER272 |
B | PRO299 |
B | SER300 |
B | TYR305 |
B | MET402 |
B | HOH509 |
B | HOH514 |
B | HOH565 |
site_id | AC4 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE MET B 402 |
Chain | Residue |
B | THR68 |
B | ASN69 |
B | GLY70 |
B | ASN71 |
B | THR72 |
B | MET119 |
B | GLN142 |
B | GLY228 |
B | PLP502 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000305|PubMed:11023792 |
Chain | Residue | Details |
A | SER8 | |
B | SER8 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: in other chain => ECO:0000305|PubMed:11023792 |
Chain | Residue | Details |
A | ASN35 | |
A | ALA269 | |
B | ASN35 | |
B | ALA269 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10452898, ECO:0000269|PubMed:11023792, ECO:0000269|PubMed:9761678 |
Chain | Residue | Details |
A | THR72 | |
A | SER273 | |
B | THR72 | |
B | SER273 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: |
Chain | Residue | Details |
A | THR177 | |
B | THR177 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: N6-(pyridoxal phosphate)lysine |
Chain | Residue | Details |
A | CYS42 | |
B | CYS42 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1oas |
Chain | Residue | Details |
A | SER272 | |
A | ALA41 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1oas |
Chain | Residue | Details |
B | SER272 | |
B | ALA41 |
site_id | CSA3 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1oas |
Chain | Residue | Details |
A | ALA41 |
site_id | CSA4 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1oas |
Chain | Residue | Details |
B | ALA41 |
site_id | MCSA1 |
Number of Residues | 2 |
Details | M-CSA 865 |
Chain | Residue | Details |
A | CYS42 | covalent catalysis, proton shuttle (general acid/base) |
A | SER273 | electrostatic stabiliser |
site_id | MCSA2 |
Number of Residues | 2 |
Details | M-CSA 865 |
Chain | Residue | Details |
B | CYS42 | covalent catalysis, proton shuttle (general acid/base) |
B | SER273 | electrostatic stabiliser |