5LNT
Crystal structure of Arabidopsis thaliana Pdx1K166R-preI320 complex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005783 | cellular_component | endoplasmic reticulum |
| A | 0005829 | cellular_component | cytosol |
| A | 0006520 | biological_process | amino acid metabolic process |
| A | 0008615 | biological_process | pyridoxine biosynthetic process |
| A | 0009507 | cellular_component | chloroplast |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016843 | molecular_function | amine-lyase activity |
| A | 0036381 | molecular_function | pyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity |
| A | 0042819 | biological_process | vitamin B6 biosynthetic process |
| A | 0042823 | biological_process | pyridoxal phosphate biosynthetic process |
| A | 0046982 | molecular_function | protein heterodimerization activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005783 | cellular_component | endoplasmic reticulum |
| B | 0005829 | cellular_component | cytosol |
| B | 0006520 | biological_process | amino acid metabolic process |
| B | 0008615 | biological_process | pyridoxine biosynthetic process |
| B | 0009507 | cellular_component | chloroplast |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016843 | molecular_function | amine-lyase activity |
| B | 0036381 | molecular_function | pyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity |
| B | 0042819 | biological_process | vitamin B6 biosynthetic process |
| B | 0042823 | biological_process | pyridoxal phosphate biosynthetic process |
| B | 0046982 | molecular_function | protein heterodimerization activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005783 | cellular_component | endoplasmic reticulum |
| C | 0005829 | cellular_component | cytosol |
| C | 0006520 | biological_process | amino acid metabolic process |
| C | 0008615 | biological_process | pyridoxine biosynthetic process |
| C | 0009507 | cellular_component | chloroplast |
| C | 0016829 | molecular_function | lyase activity |
| C | 0016843 | molecular_function | amine-lyase activity |
| C | 0036381 | molecular_function | pyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity |
| C | 0042819 | biological_process | vitamin B6 biosynthetic process |
| C | 0042823 | biological_process | pyridoxal phosphate biosynthetic process |
| C | 0046982 | molecular_function | protein heterodimerization activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005783 | cellular_component | endoplasmic reticulum |
| D | 0005829 | cellular_component | cytosol |
| D | 0006520 | biological_process | amino acid metabolic process |
| D | 0008615 | biological_process | pyridoxine biosynthetic process |
| D | 0009507 | cellular_component | chloroplast |
| D | 0016829 | molecular_function | lyase activity |
| D | 0016843 | molecular_function | amine-lyase activity |
| D | 0036381 | molecular_function | pyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity |
| D | 0042819 | biological_process | vitamin B6 biosynthetic process |
| D | 0042823 | biological_process | pyridoxal phosphate biosynthetic process |
| D | 0046982 | molecular_function | protein heterodimerization activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 19 |
| Details | binding site for residue KPR A 401 |
| Chain | Residue |
| A | ASP41 |
| A | GLY170 |
| A | ALA229 |
| A | GLY230 |
| A | GLY231 |
| A | PHE250 |
| A | GLY252 |
| A | SER253 |
| A | HOH504 |
| A | HOH509 |
| A | HOH544 |
| A | PRO66 |
| A | LYS98 |
| A | ASP119 |
| A | SER121 |
| A | VAL123 |
| A | ARG164 |
| A | GLU168 |
| A | ALA169 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue PO4 A 402 |
| Chain | Residue |
| A | HIS132 |
| A | GLU151 |
| A | ARG154 |
| A | ARG155 |
| A | HOH587 |
| D | LYS204 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue PO4 B 402 |
| Chain | Residue |
| B | HIS132 |
| B | GLU151 |
| B | ARG154 |
| B | ARG155 |
| B | HOH589 |
| C | LYS204 |
| C | HOH582 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue PO4 C 402 |
| Chain | Residue |
| B | LYS204 |
| C | HIS132 |
| C | GLU151 |
| C | ARG154 |
| C | ARG155 |
| C | HOH508 |
| C | HOH588 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue PO4 D 402 |
| Chain | Residue |
| A | LYS204 |
| D | HIS132 |
| D | GLU151 |
| D | ARG154 |
| D | ARG155 |
| site_id | AC6 |
| Number of Residues | 26 |
| Details | binding site for Di-peptide KPR B 401 and LYS B 98 |
| Chain | Residue |
| B | ASP41 |
| B | ALA61 |
| B | LEU62 |
| B | PRO66 |
| B | MET78 |
| B | ALA97 |
| B | ALA99 |
| B | LEU110 |
| B | ASP119 |
| B | SER121 |
| B | VAL123 |
| B | LEU124 |
| B | ARG164 |
| B | GLU168 |
| B | ALA169 |
| B | GLY170 |
| B | ALA229 |
| B | GLY230 |
| B | GLY231 |
| B | PHE250 |
| B | GLY252 |
| B | SER253 |
| B | HOH511 |
| B | HOH521 |
| B | HOH524 |
| B | HOH532 |
| site_id | AC7 |
| Number of Residues | 27 |
| Details | binding site for Di-peptide KPR C 401 and LYS C 98 |
| Chain | Residue |
| C | ASP41 |
| C | MET60 |
| C | ALA61 |
| C | LEU62 |
| C | PRO66 |
| C | MET78 |
| C | ALA97 |
| C | ALA99 |
| C | ASP119 |
| C | SER121 |
| C | VAL123 |
| C | LEU124 |
| C | ARG164 |
| C | GLU168 |
| C | ALA169 |
| C | GLY170 |
| C | ALA229 |
| C | GLY230 |
| C | GLY231 |
| C | PHE250 |
| C | VAL251 |
| C | GLY252 |
| C | SER253 |
| C | HOH510 |
| C | HOH515 |
| C | HOH530 |
| C | HOH550 |
| site_id | AC8 |
| Number of Residues | 26 |
| Details | binding site for Di-peptide KPR D 401 and LYS D 98 |
| Chain | Residue |
| D | ALA61 |
| D | LEU62 |
| D | PRO66 |
| D | ALA97 |
| D | ALA99 |
| D | LEU110 |
| D | ASP119 |
| D | SER121 |
| D | VAL123 |
| D | LEU124 |
| D | ARG164 |
| D | GLU168 |
| D | ALA169 |
| D | GLY170 |
| D | ALA229 |
| D | GLY230 |
| D | GLY231 |
| D | PHE250 |
| D | GLY252 |
| D | SER253 |
| D | HOH511 |
| D | HOH515 |
| D | HOH521 |
| D | HOH559 |
| D | ASP41 |
| D | MET60 |
Functional Information from PROSITE/UniProt
| site_id | PS01235 |
| Number of Residues | 19 |
| Details | PDXS_SNZ_1 PdxS/SNZ family signature. LPVVQFAAGGVATPADAAL |
| Chain | Residue | Details |
| A | LEU222-LEU240 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Schiff-base intermediate with D-ribose 5-phosphate => ECO:0000250|UniProtKB:O59080 |
| Chain | Residue | Details |
| A | LYS98 | |
| B | LYS98 | |
| C | LYS98 | |
| D | LYS98 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:O59080 |
| Chain | Residue | Details |
| A | ASP41 | |
| C | GLY170 | |
| C | GLY231 | |
| C | GLY252 | |
| D | ASP41 | |
| D | GLY170 | |
| D | GLY231 | |
| D | GLY252 | |
| A | GLY170 | |
| A | GLY231 | |
| A | GLY252 | |
| B | ASP41 | |
| B | GLY170 | |
| B | GLY231 | |
| B | GLY252 | |
| C | ASP41 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q03148 |
| Chain | Residue | Details |
| A | ARG182 | |
| B | ARG182 | |
| C | ARG182 | |
| D | ARG182 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | MOD_RES: N-acetylmethionine => ECO:0000250|UniProtKB:Q8L940 |
| Chain | Residue | Details |
| A | MET1 | |
| B | MET1 | |
| C | MET1 | |
| D | MET1 |
