2C2B
Crystallographic structure of Arabidopsis thaliana Threonine synthase complexed with pyridoxal phosphate and S-adenosylmethionine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004795 | molecular_function | threonine synthase activity |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006520 | biological_process | amino acid metabolic process |
| A | 0009088 | biological_process | threonine biosynthetic process |
| A | 0009507 | cellular_component | chloroplast |
| A | 0009570 | cellular_component | chloroplast stroma |
| A | 0016829 | molecular_function | lyase activity |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0004795 | molecular_function | threonine synthase activity |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0006520 | biological_process | amino acid metabolic process |
| B | 0009088 | biological_process | threonine biosynthetic process |
| B | 0009507 | cellular_component | chloroplast |
| B | 0009570 | cellular_component | chloroplast stroma |
| B | 0016829 | molecular_function | lyase activity |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| C | 0004795 | molecular_function | threonine synthase activity |
| C | 0005886 | cellular_component | plasma membrane |
| C | 0006520 | biological_process | amino acid metabolic process |
| C | 0009088 | biological_process | threonine biosynthetic process |
| C | 0009507 | cellular_component | chloroplast |
| C | 0009570 | cellular_component | chloroplast stroma |
| C | 0016829 | molecular_function | lyase activity |
| C | 0030170 | molecular_function | pyridoxal phosphate binding |
| D | 0004795 | molecular_function | threonine synthase activity |
| D | 0005886 | cellular_component | plasma membrane |
| D | 0006520 | biological_process | amino acid metabolic process |
| D | 0009088 | biological_process | threonine biosynthetic process |
| D | 0009507 | cellular_component | chloroplast |
| D | 0009570 | cellular_component | chloroplast stroma |
| D | 0016829 | molecular_function | lyase activity |
| D | 0030170 | molecular_function | pyridoxal phosphate binding |
| E | 0004795 | molecular_function | threonine synthase activity |
| E | 0005886 | cellular_component | plasma membrane |
| E | 0006520 | biological_process | amino acid metabolic process |
| E | 0009088 | biological_process | threonine biosynthetic process |
| E | 0009507 | cellular_component | chloroplast |
| E | 0009570 | cellular_component | chloroplast stroma |
| E | 0016829 | molecular_function | lyase activity |
| E | 0030170 | molecular_function | pyridoxal phosphate binding |
| F | 0004795 | molecular_function | threonine synthase activity |
| F | 0005886 | cellular_component | plasma membrane |
| F | 0006520 | biological_process | amino acid metabolic process |
| F | 0009088 | biological_process | threonine biosynthetic process |
| F | 0009507 | cellular_component | chloroplast |
| F | 0009570 | cellular_component | chloroplast stroma |
| F | 0016829 | molecular_function | lyase activity |
| F | 0030170 | molecular_function | pyridoxal phosphate binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PLP A 1163 |
| Chain | Residue |
| A | PHE162 |
| A | ALA356 |
| A | HIS404 |
| A | THR432 |
| A | ALA433 |
| A | HOH2025 |
| A | LYS163 |
| A | ASP194 |
| A | GLY294 |
| A | GLY295 |
| A | ASN296 |
| A | LEU297 |
| A | GLY298 |
| A | ASN299 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PLP B 1163 |
| Chain | Residue |
| B | LYS163 |
| B | SER191 |
| B | THR195 |
| B | SER262 |
| B | ARG267 |
| B | GLN271 |
| B | ASN296 |
| B | ASN299 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PLP C 1163 |
| Chain | Residue |
| C | PHE162 |
| C | LYS163 |
| C | ASP194 |
| C | GLY294 |
| C | GLY295 |
| C | ASN296 |
| C | LEU297 |
| C | GLY298 |
| C | ASN299 |
| C | ALA356 |
| C | HIS404 |
| C | THR432 |
| C | ALA433 |
| C | HOH2038 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PLP D 1163 |
| Chain | Residue |
| D | PHE162 |
| D | LYS163 |
| D | SER191 |
| D | ASP194 |
| D | THR195 |
| D | SER262 |
| D | ARG267 |
| D | GLN271 |
| D | ASN296 |
| D | ASN299 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PLP E 1163 |
| Chain | Residue |
| E | PHE162 |
| E | LYS163 |
| E | SER191 |
| E | ASP194 |
| E | THR195 |
| E | SER262 |
| E | ARG267 |
| E | GLN271 |
| E | ASN296 |
| E | ASN299 |
| site_id | AC6 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PLP F 1163 |
| Chain | Residue |
| F | PHE162 |
| F | LYS163 |
| F | ASP194 |
| F | GLY294 |
| F | GLY295 |
| F | ASN296 |
| F | LEU297 |
| F | GLY298 |
| F | ASN299 |
| F | ALA356 |
| F | HIS404 |
| F | THR432 |
| F | ALA433 |
| F | HOH2046 |
| site_id | AC7 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE SAM A 500 |
| Chain | Residue |
| A | SER99 |
| A | THR100 |
| A | TRP101 |
| A | PRO102 |
| A | GLY104 |
| A | SER105 |
| A | SER125 |
| A | PHE127 |
| A | SAM501 |
| B | ASN132 |
| B | LEU133 |
| B | TRP150 |
| B | GLN281 |
| B | PHE282 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SAM A 501 |
| Chain | Residue |
| A | TRP101 |
| A | SAM500 |
| A | HOH2051 |
| B | TRP135 |
| B | LYS141 |
| B | ASN147 |
| B | TRP150 |
| site_id | AC9 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE SAM B 500 |
| Chain | Residue |
| B | GLY104 |
| B | SER105 |
| B | SER125 |
| B | PHE127 |
| B | SAM501 |
| A | ASN132 |
| A | LEU133 |
| A | TRP150 |
| A | GLN281 |
| B | SER99 |
| B | THR100 |
| B | TRP101 |
| B | PRO102 |
| site_id | BC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SAM B 501 |
| Chain | Residue |
| A | TRP135 |
| A | LYS141 |
| A | ASN147 |
| A | TRP150 |
| B | TRP101 |
| B | SAM500 |
| B | HOH2055 |
| E | ASP343 |
| site_id | BC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE SAM C 500 |
| Chain | Residue |
| C | SER99 |
| C | THR100 |
| C | TRP101 |
| C | PRO102 |
| C | GLY104 |
| C | SER105 |
| C | SER125 |
| C | PHE127 |
| C | SAM501 |
| D | ASN132 |
| D | LEU133 |
| D | TRP150 |
| D | GLN281 |
| D | PHE282 |
| site_id | BC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SAM C 501 |
| Chain | Residue |
| C | TRP101 |
| C | SAM500 |
| C | HOH2051 |
| C | HOH2052 |
| D | TRP135 |
| D | LYS141 |
| D | ASN147 |
| D | TRP150 |
| site_id | BC4 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE SAM D 500 |
| Chain | Residue |
| C | ASN132 |
| C | LEU133 |
| C | TRP150 |
| C | GLN281 |
| C | PHE282 |
| D | SER99 |
| D | THR100 |
| D | TRP101 |
| D | PRO102 |
| D | GLY104 |
| D | SER105 |
| D | SER125 |
| D | PHE127 |
| D | SAM501 |
| site_id | BC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SAM D 501 |
| Chain | Residue |
| C | TRP135 |
| C | LYS141 |
| C | TRP150 |
| D | TRP101 |
| D | ASP343 |
| D | SAM500 |
| D | HOH2054 |
| site_id | BC6 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE SAM E 500 |
| Chain | Residue |
| E | SER99 |
| E | THR100 |
| E | TRP101 |
| E | PRO102 |
| E | GLY104 |
| E | SER125 |
| E | PHE127 |
| E | SAM501 |
| F | ASN132 |
| F | LEU133 |
| F | TRP150 |
| F | GLN281 |
| F | ASP283 |
| site_id | BC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SAM E 501 |
| Chain | Residue |
| B | ASP343 |
| E | TRP101 |
| E | SAM500 |
| E | HOH2044 |
| F | TRP135 |
| F | LYS141 |
| F | ASN147 |
| site_id | BC8 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE SAM F 500 |
| Chain | Residue |
| E | ASN132 |
| E | LEU133 |
| E | TRP150 |
| E | GLN281 |
| E | PHE282 |
| F | SER99 |
| F | THR100 |
| F | TRP101 |
| F | PRO102 |
| F | TYR103 |
| F | GLY104 |
| F | SER105 |
| F | SER125 |
| F | PHE127 |
| F | SAM501 |
| site_id | BC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SAM F 501 |
| Chain | Residue |
| E | TRP135 |
| E | LYS141 |
| E | ASN147 |
| E | TRP150 |
| F | TRP101 |
| F | SAM500 |
| F | HOH2056 |
| site_id | CC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE TRS A 800 |
| Chain | Residue |
| A | ASP122 |
| site_id | CC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE TRS C 800 |
| Chain | Residue |
| C | ASP119 |
| C | ASP122 |
| site_id | CC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE TRS F 800 |
| Chain | Residue |
| F | ASP119 |
| F | ASP122 |
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 | 12 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | PRO102 | |
| E | SER125 | |
| F | PRO102 | |
| F | SER125 | |
| A | SER125 | |
| B | PRO102 | |
| B | SER125 | |
| C | PRO102 | |
| C | SER125 | |
| D | PRO102 | |
| D | SER125 | |
| E | PRO102 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:16319072 |
| Chain | Residue | Details |
| A | ASN132 | |
| E | LEU133 | |
| F | ASN132 | |
| F | LEU133 | |
| A | LEU133 | |
| B | ASN132 | |
| B | LEU133 | |
| C | ASN132 | |
| C | LEU133 | |
| D | ASN132 | |
| D | LEU133 | |
| E | ASN132 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | BINDING: in monomer A => ECO:0000269|PubMed:16319072 |
| Chain | Residue | Details |
| A | LYS141 | |
| B | LYS141 | |
| C | LYS141 | |
| D | LYS141 | |
| E | LYS141 | |
| F | LYS141 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | BINDING: in monomer B => ECO:0000269|PubMed:16319072 |
| Chain | Residue | Details |
| A | ASN147 | |
| B | ASN147 | |
| C | ASN147 | |
| D | ASN147 | |
| E | ASN147 | |
| F | ASN147 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | GLY295 | |
| E | THR432 | |
| F | GLY295 | |
| F | THR432 | |
| A | THR432 | |
| B | GLY295 | |
| B | THR432 | |
| C | GLY295 | |
| C | THR432 | |
| D | GLY295 | |
| D | THR432 | |
| E | GLY295 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 6 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine |
| Chain | Residue | Details |
| A | LYS163 | |
| B | LYS163 | |
| C | LYS163 | |
| D | LYS163 | |
| E | LYS163 | |
| F | LYS163 |
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 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1tdj |
| Chain | Residue | Details |
| C | SER431 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1tdj |
| Chain | Residue | Details |
| D | SER431 |
| site_id | CSA5 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1tdj |
| Chain | Residue | Details |
| E | SER431 |
| site_id | CSA6 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1tdj |
| Chain | Residue | Details |
| F | SER431 |
