2C2G
Crystal structure of Threonine Synthase from Arabidopsis thaliana in complex with its cofactor pyridoxal phosphate
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0004795 | molecular_function | threonine synthase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0005886 | cellular_component | plasma membrane |
A | 0006520 | biological_process | amino acid metabolic process |
A | 0008652 | biological_process | amino acid biosynthetic process |
A | 0009088 | biological_process | threonine biosynthetic process |
A | 0009507 | cellular_component | chloroplast |
A | 0009570 | cellular_component | chloroplast stroma |
A | 0010073 | biological_process | meristem maintenance |
A | 0016829 | molecular_function | lyase activity |
A | 0019344 | biological_process | cysteine biosynthetic process |
A | 0030170 | molecular_function | pyridoxal phosphate binding |
B | 0003824 | molecular_function | catalytic activity |
B | 0004795 | molecular_function | threonine synthase activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0005886 | cellular_component | plasma membrane |
B | 0006520 | biological_process | amino acid metabolic process |
B | 0008652 | biological_process | amino acid biosynthetic process |
B | 0009088 | biological_process | threonine biosynthetic process |
B | 0009507 | cellular_component | chloroplast |
B | 0009570 | cellular_component | chloroplast stroma |
B | 0010073 | biological_process | meristem maintenance |
B | 0016829 | molecular_function | lyase activity |
B | 0019344 | biological_process | cysteine biosynthetic process |
B | 0030170 | molecular_function | pyridoxal phosphate binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE PLP A 1163 |
Chain | Residue |
A | LYS163 |
A | SER191 |
A | THR195 |
A | SER262 |
A | ARG267 |
A | GLN271 |
A | ASN296 |
A | ASN299 |
site_id | AC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE PLP B 1163 |
Chain | Residue |
B | SER191 |
B | THR195 |
B | SER262 |
B | ARG267 |
B | GLN271 |
B | ASN296 |
B | ASN299 |
B | LYS163 |
Functional Information from PROSITE/UniProt
site_id | PS00165 |
Number of Residues | 15 |
Details | DEHYDRATASE_SER_THR Serine/threonine dehydratases pyridoxal-phosphate attachment site. HcgishTGSFKDLGM |
Chain | Residue | Details |
A | HIS153-MET167 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 8 |
Details | Binding site: {} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"16319072","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | Binding site: {"description":"in monomer A","evidences":[{"source":"PubMed","id":"16319072","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | Binding site: {"description":"in monomer B","evidences":[{"source":"PubMed","id":"16319072","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 10 |
Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine"} |
Chain | Residue | Details |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1tdj |
Chain | Residue | Details |
A | SER431 |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1tdj |
Chain | Residue | Details |
B | SER431 |