6HX3
PDX1.2/PDX1.3 complex
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005515 | molecular_function | protein binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0042819 | biological_process | vitamin B6 biosynthetic process |
A | 0042823 | biological_process | pyridoxal phosphate biosynthetic process |
A | 0046982 | molecular_function | protein heterodimerization activity |
B | 0042819 | biological_process | vitamin B6 biosynthetic process |
B | 0042823 | biological_process | pyridoxal phosphate biosynthetic process |
C | 0005515 | molecular_function | protein binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0005829 | cellular_component | cytosol |
C | 0042819 | biological_process | vitamin B6 biosynthetic process |
C | 0042823 | biological_process | pyridoxal phosphate biosynthetic process |
C | 0046982 | molecular_function | protein heterodimerization activity |
D | 0042819 | biological_process | vitamin B6 biosynthetic process |
D | 0042823 | biological_process | pyridoxal phosphate biosynthetic process |
E | 0005515 | molecular_function | protein binding |
E | 0005737 | cellular_component | cytoplasm |
E | 0005829 | cellular_component | cytosol |
E | 0042819 | biological_process | vitamin B6 biosynthetic process |
E | 0042823 | biological_process | pyridoxal phosphate biosynthetic process |
E | 0046982 | molecular_function | protein heterodimerization activity |
F | 0042819 | biological_process | vitamin B6 biosynthetic process |
F | 0042823 | biological_process | pyridoxal phosphate biosynthetic process |
G | 0005515 | molecular_function | protein binding |
G | 0005737 | cellular_component | cytoplasm |
G | 0005829 | cellular_component | cytosol |
G | 0042819 | biological_process | vitamin B6 biosynthetic process |
G | 0042823 | biological_process | pyridoxal phosphate biosynthetic process |
G | 0046982 | molecular_function | protein heterodimerization activity |
H | 0042819 | biological_process | vitamin B6 biosynthetic process |
H | 0042823 | biological_process | pyridoxal phosphate biosynthetic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 11 |
Details | binding site for residue SO4 A 401 |
Chain | Residue |
A | PHE135 |
D | LYS203 |
D | HOH416 |
A | GLU154 |
A | ARG157 |
A | ARG158 |
B | HIS131 |
B | GLU150 |
B | ARG153 |
B | ARG154 |
C | LYS208 |
site_id | AC2 |
Number of Residues | 9 |
Details | binding site for residue SO4 C 401 |
Chain | Residue |
A | LYS208 |
A | HOH531 |
B | LYS203 |
C | PHE135 |
C | ARG157 |
C | ARG158 |
D | HIS131 |
D | ARG153 |
D | ARG154 |
site_id | AC3 |
Number of Residues | 9 |
Details | binding site for residue SO4 C 402 |
Chain | Residue |
C | GLU48 |
C | THR173 |
C | GLY235 |
C | GLY256 |
D | GLU167 |
D | ALA168 |
D | GLY169 |
D | GLY230 |
D | GLY251 |
site_id | AC4 |
Number of Residues | 10 |
Details | binding site for residue SO4 E 401 |
Chain | Residue |
E | PHE135 |
E | GLU154 |
E | ARG157 |
E | ARG158 |
E | HOH505 |
F | GLU150 |
F | ARG153 |
F | ARG154 |
G | LYS208 |
H | LYS203 |
site_id | AC5 |
Number of Residues | 10 |
Details | binding site for residue SO4 G 401 |
Chain | Residue |
E | LYS208 |
E | HOH524 |
F | LYS203 |
G | PHE135 |
G | ARG157 |
G | ARG158 |
H | HIS131 |
H | GLU150 |
H | ARG153 |
H | ARG154 |
site_id | AC6 |
Number of Residues | 7 |
Details | binding site for residue SO4 B 301 |
Chain | Residue |
A | ILE127 |
A | SER128 |
A | VAL129 |
B | LEU123 |
B | THR124 |
B | LEU125 |
B | HOH402 |
site_id | AC7 |
Number of Residues | 12 |
Details | binding site for residue SO4 B 302 |
Chain | Residue |
A | THR173 |
A | GLY234 |
A | GLY235 |
A | GLY256 |
A | HOH508 |
B | LYS165 |
B | GLU167 |
B | ALA168 |
B | GLY169 |
B | GLY229 |
B | GLY230 |
B | GLY251 |
site_id | AC8 |
Number of Residues | 6 |
Details | binding site for residue SO4 D 301 |
Chain | Residue |
C | ILE127 |
C | VAL129 |
D | LEU123 |
D | THR124 |
D | LEU125 |
D | HOH404 |
site_id | AC9 |
Number of Residues | 7 |
Details | binding site for residue SO4 F 301 |
Chain | Residue |
E | ILE127 |
E | SER128 |
E | VAL129 |
F | LEU123 |
F | THR124 |
F | LEU125 |
F | HOH410 |
site_id | AD1 |
Number of Residues | 9 |
Details | binding site for residue SO4 F 302 |
Chain | Residue |
E | GLU48 |
E | THR173 |
E | GLY235 |
E | GLY256 |
F | GLU167 |
F | ALA168 |
F | GLY169 |
F | GLY230 |
F | GLY251 |
site_id | AD2 |
Number of Residues | 8 |
Details | binding site for residue SO4 H 301 |
Chain | Residue |
G | ILE127 |
G | SER128 |
G | VAL129 |
H | LEU123 |
H | THR124 |
H | LEU125 |
H | HOH406 |
H | HOH420 |
site_id | AD3 |
Number of Residues | 10 |
Details | binding site for residue SO4 H 302 |
Chain | Residue |
G | GLY234 |
G | GLY235 |
G | GLY256 |
H | GLU167 |
H | ALA168 |
H | GLY169 |
H | GLY229 |
H | GLY230 |
H | GLY251 |
G | ASP171 |
Functional Information from PROSITE/UniProt
site_id | PS01235 |
Number of Residues | 19 |
Details | PDXS_SNZ_1 PdxS/SNZ family signature. VPVVQFASGGITTPADAAL |
Chain | Residue | Details |
A | VAL226-LEU244 | |
B | LEU221-LEU239 |
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 |
B | LYS97 | |
D | LYS97 | |
F | LYS97 | |
H | LYS97 |
site_id | SWS_FT_FI2 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:O59080 |
Chain | Residue | Details |
B | ASP40 | |
F | GLY169 | |
F | GLY230 | |
F | GLY251 | |
H | ASP40 | |
H | GLY169 | |
H | GLY230 | |
H | GLY251 | |
B | GLY169 | |
B | GLY230 | |
B | GLY251 | |
D | ASP40 | |
D | GLY169 | |
D | GLY230 | |
D | GLY251 | |
F | ASP40 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q03148 |
Chain | Residue | Details |
B | ARG181 | |
D | ARG181 | |
F | ARG181 | |
H | ARG181 |