2CB1
Crystal Structure of O-actetyl Homoserine Sulfhydrylase From Thermus Thermophilus HB8,OAH2.
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0003961 | molecular_function | O-acetylhomoserine aminocarboxypropyltransferase activity |
A | 0004124 | molecular_function | cysteine synthase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0006520 | biological_process | amino acid metabolic process |
A | 0006535 | biological_process | cysteine biosynthetic process from serine |
A | 0008652 | biological_process | amino acid biosynthetic process |
A | 0009086 | biological_process | methionine biosynthetic process |
A | 0016740 | molecular_function | transferase activity |
A | 0016765 | molecular_function | transferase activity, transferring alkyl or aryl (other than methyl) groups |
A | 0019346 | biological_process | transsulfuration |
A | 0030170 | molecular_function | pyridoxal phosphate binding |
A | 0051009 | molecular_function | O-acetylhomoserine sulfhydrylase activity |
A | 0071266 | biological_process | 'de novo' L-methionine biosynthetic process |
A | 0071269 | biological_process | L-homocysteine biosynthetic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE PLP A 1202 |
Chain | Residue |
A | TYR50 |
A | THR201 |
A | LYS202 |
A | GLY212 |
A | ARG52 |
A | SER79 |
A | GLY80 |
A | GLN81 |
A | PHE105 |
A | ASP176 |
A | THR178 |
A | SER199 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2005","submissionDatabase":"PDB data bank","title":"The crystal structure of O-acetyl homoserine sulfhydrylase.","authors":["Agari Y.","Satoh S.","Tsuge H.","Imagawa T.","Utsunomiya H."]}},{"source":"PDB","id":"2CB1","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ay4 |
Chain | Residue | Details |
A | PHE105 | |
A | ASP176 |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1ay4 |
Chain | Residue | Details |
A | ARG52 |