6H0N
The structure of wild-type Arabidopsis thaliana UDP-apiose/UDP-xylose synthase in complex with NAD+ and UDP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005777 | cellular_component | peroxisome |
| A | 0005829 | cellular_component | cytosol |
| A | 0009226 | biological_process | nucleotide-sugar biosynthetic process |
| A | 0010396 | biological_process | rhamnogalacturonan II metabolic process |
| A | 0010494 | cellular_component | cytoplasmic stress granule |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016831 | molecular_function | carboxy-lyase activity |
| A | 0033320 | biological_process | UDP-D-xylose biosynthetic process |
| A | 0033352 | biological_process | UDP-D-apiose biosynthetic process |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0046982 | molecular_function | protein heterodimerization activity |
| A | 0048040 | molecular_function | UDP-glucuronate decarboxylase activity |
| A | 0051287 | molecular_function | NAD binding |
| A | 0071555 | biological_process | cell wall organization |
| A | 0102765 | molecular_function | UDP-D-apiose synthase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005777 | cellular_component | peroxisome |
| B | 0005829 | cellular_component | cytosol |
| B | 0009226 | biological_process | nucleotide-sugar biosynthetic process |
| B | 0010396 | biological_process | rhamnogalacturonan II metabolic process |
| B | 0010494 | cellular_component | cytoplasmic stress granule |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016831 | molecular_function | carboxy-lyase activity |
| B | 0033320 | biological_process | UDP-D-xylose biosynthetic process |
| B | 0033352 | biological_process | UDP-D-apiose biosynthetic process |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0046982 | molecular_function | protein heterodimerization activity |
| B | 0048040 | molecular_function | UDP-glucuronate decarboxylase activity |
| B | 0051287 | molecular_function | NAD binding |
| B | 0071555 | biological_process | cell wall organization |
| B | 0102765 | molecular_function | UDP-D-apiose synthase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 24 |
| Details | binding site for residue NAD A 401 |
| Chain | Residue |
| A | GLY24 |
| A | ILE77 |
| A | LEU96 |
| A | ALA97 |
| A | ALA98 |
| A | CYS100 |
| A | PHE137 |
| A | SER138 |
| A | THR139 |
| A | TYR185 |
| A | LYS189 |
| A | GLY26 |
| A | PRO212 |
| A | ASN214 |
| A | TRP215 |
| A | ARG235 |
| A | PO4403 |
| A | GLY27 |
| A | PHE28 |
| A | ILE29 |
| A | ASP49 |
| A | VAL50 |
| A | ILE75 |
| A | ASN76 |
| site_id | AC2 |
| Number of Residues | 18 |
| Details | binding site for residue UDP A 402 |
| Chain | Residue |
| A | PRO102 |
| A | GLU141 |
| A | ARG182 |
| A | ASN214 |
| A | ARG235 |
| A | VAL236 |
| A | CYS239 |
| A | LYS251 |
| A | LEU252 |
| A | VAL253 |
| A | ARG260 |
| A | VAL298 |
| A | PHE330 |
| A | TYR331 |
| A | TYR335 |
| A | ASP337 |
| A | ARG341 |
| A | PO4403 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | binding site for residue PO4 A 403 |
| Chain | Residue |
| A | CYS100 |
| A | TYR105 |
| A | THR139 |
| A | GLU141 |
| A | TYR185 |
| A | ARG235 |
| A | NAD401 |
| A | UDP402 |
| site_id | AC4 |
| Number of Residues | 22 |
| Details | binding site for residue NAD B 401 |
| Chain | Residue |
| B | GLY24 |
| B | GLY26 |
| B | GLY27 |
| B | PHE28 |
| B | ILE29 |
| B | ASP49 |
| B | ILE75 |
| B | ASN76 |
| B | ILE77 |
| B | LEU96 |
| B | ALA97 |
| B | ALA98 |
| B | CYS100 |
| B | PHE137 |
| B | SER138 |
| B | THR139 |
| B | TYR185 |
| B | LYS189 |
| B | PRO212 |
| B | TRP215 |
| B | ARG235 |
| B | PO4403 |
| site_id | AC5 |
| Number of Residues | 18 |
| Details | binding site for residue UDP B 402 |
| Chain | Residue |
| B | PRO102 |
| B | GLU141 |
| B | ARG182 |
| B | ASN214 |
| B | ARG235 |
| B | VAL236 |
| B | CYS239 |
| B | LYS251 |
| B | LEU252 |
| B | VAL253 |
| B | ARG260 |
| B | VAL298 |
| B | PHE330 |
| B | TYR331 |
| B | TYR335 |
| B | ASP337 |
| B | ARG341 |
| B | PO4403 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | binding site for residue PO4 B 403 |
| Chain | Residue |
| B | CYS100 |
| B | TYR105 |
| B | THR139 |
| B | GLU141 |
| B | TYR185 |
| B | ARG235 |
| B | NAD401 |
| B | UDP402 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000269|PubMed:31844840 |
| Chain | Residue | Details |
| A | TYR185 | |
| B | TYR185 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 28 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:31844840, ECO:0007744|PDB:6H0N, ECO:0007744|PDB:6H0P |
| Chain | Residue | Details |
| A | PHE28 | |
| A | VAL253 | |
| A | ARG260 | |
| A | TYR335 | |
| A | ASP337 | |
| A | ARG341 | |
| B | PHE28 | |
| B | ILE29 | |
| B | ASN76 | |
| B | ILE77 | |
| B | ARG182 | |
| A | ILE29 | |
| B | LYS189 | |
| B | ASN214 | |
| B | ARG235 | |
| B | LYS251 | |
| B | VAL253 | |
| B | ARG260 | |
| B | TYR335 | |
| B | ASP337 | |
| B | ARG341 | |
| A | ASN76 | |
| A | ILE77 | |
| A | ARG182 | |
| A | LYS189 | |
| A | ASN214 | |
| A | ARG235 | |
| A | LYS251 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:31844840, ECO:0007744|PDB:6H0N |
| Chain | Residue | Details |
| A | ASP49 | |
| A | LEU96 | |
| A | TRP215 | |
| B | ASP49 | |
| B | LEU96 | |
| B | TRP215 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:31844840, ECO:0007744|PDB:6H0P |
| Chain | Residue | Details |
| A | TYR105 | |
| B | TYR331 | |
| A | THR139 | |
| A | GLU141 | |
| A | TYR185 | |
| A | TYR331 | |
| B | TYR105 | |
| B | THR139 | |
| B | GLU141 | |
| B | TYR185 |
