7WKW
NPA bound state of AtPIN3
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005739 | cellular_component | mitochondrion |
A | 0005783 | cellular_component | endoplasmic reticulum |
A | 0005886 | cellular_component | plasma membrane |
A | 0009416 | biological_process | response to light stimulus |
A | 0009606 | biological_process | tropism |
A | 0009630 | biological_process | gravitropism |
A | 0009734 | biological_process | auxin-activated signaling pathway |
A | 0009926 | biological_process | auxin polar transport |
A | 0009958 | biological_process | positive gravitropism |
A | 0009986 | cellular_component | cell surface |
A | 0010315 | biological_process | auxin export across the plasma membrane |
A | 0010329 | molecular_function | auxin efflux transmembrane transporter activity |
A | 0012506 | cellular_component | vesicle membrane |
A | 0016020 | cellular_component | membrane |
A | 0016328 | cellular_component | lateral plasma membrane |
A | 0042802 | molecular_function | identical protein binding |
A | 0042803 | molecular_function | protein homodimerization activity |
A | 0048364 | biological_process | root development |
A | 0048766 | biological_process | root hair initiation |
A | 0048767 | biological_process | root hair elongation |
A | 0055085 | biological_process | transmembrane transport |
A | 0060918 | biological_process | auxin transport |
A | 0071469 | biological_process | cellular response to alkaline pH |
B | 0005739 | cellular_component | mitochondrion |
B | 0005783 | cellular_component | endoplasmic reticulum |
B | 0005886 | cellular_component | plasma membrane |
B | 0009416 | biological_process | response to light stimulus |
B | 0009606 | biological_process | tropism |
B | 0009630 | biological_process | gravitropism |
B | 0009734 | biological_process | auxin-activated signaling pathway |
B | 0009926 | biological_process | auxin polar transport |
B | 0009958 | biological_process | positive gravitropism |
B | 0009986 | cellular_component | cell surface |
B | 0010315 | biological_process | auxin export across the plasma membrane |
B | 0010329 | molecular_function | auxin efflux transmembrane transporter activity |
B | 0012506 | cellular_component | vesicle membrane |
B | 0016020 | cellular_component | membrane |
B | 0016328 | cellular_component | lateral plasma membrane |
B | 0042802 | molecular_function | identical protein binding |
B | 0042803 | molecular_function | protein homodimerization activity |
B | 0048364 | biological_process | root development |
B | 0048766 | biological_process | root hair initiation |
B | 0048767 | biological_process | root hair elongation |
B | 0055085 | biological_process | transmembrane transport |
B | 0060918 | biological_process | auxin transport |
B | 0071469 | biological_process | cellular response to alkaline pH |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 62 |
Details | TOPO_DOM: Extracellular => ECO:0000305 |
Chain | Residue | Details |
B | MET1-LEU7 | |
A | GLY581-ASP585 | |
B | SER60-PHE71 | |
B | ALA123-SER131 | |
B | GLN522-SER524 | |
B | GLY581-ASP585 | |
A | MET1-LEU7 | |
A | SER60-PHE71 | |
A | ALA123-SER131 | |
A | GLN522-SER524 |
site_id | SWS_FT_FI2 |
Number of Residues | 40 |
Details | TRANSMEM: Helical; Name=1 => ECO:0000255 |
Chain | Residue | Details |
B | TYR8-VAL28 | |
A | TYR8-VAL28 |
site_id | SWS_FT_FI3 |
Number of Residues | 778 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000305 |
Chain | Residue | Details |
B | ARG29-GLN38 | |
A | LYS607-GLY619 | |
B | THR93-SER101 | |
B | GLU153-SER500 | |
B | LEU546-THR559 | |
B | LYS607-GLY619 | |
A | ARG29-GLN38 | |
A | THR93-SER101 | |
A | GLU153-SER500 | |
A | LEU546-THR559 |
site_id | SWS_FT_FI4 |
Number of Residues | 40 |
Details | TRANSMEM: Helical; Name=2 => ECO:0000255 |
Chain | Residue | Details |
B | CYS39-ILE59 | |
A | CYS39-ILE59 |
site_id | SWS_FT_FI5 |
Number of Residues | 40 |
Details | TRANSMEM: Helical; Name=3 => ECO:0000255 |
Chain | Residue | Details |
B | ILE72-PHE92 | |
A | ILE72-PHE92 |
site_id | SWS_FT_FI6 |
Number of Residues | 40 |
Details | TRANSMEM: Helical; Name=4 => ECO:0000255 |
Chain | Residue | Details |
B | ILE102-ILE122 | |
A | ILE102-ILE122 |
site_id | SWS_FT_FI7 |
Number of Residues | 40 |
Details | TRANSMEM: Helical; Name=5 => ECO:0000255 |
Chain | Residue | Details |
B | LEU132-PHE152 | |
A | LEU132-PHE152 |
site_id | SWS_FT_FI8 |
Number of Residues | 40 |
Details | TRANSMEM: Helical; Name=6 => ECO:0000255 |
Chain | Residue | Details |
B | LEU501-ILE521 | |
A | LEU501-ILE521 |
site_id | SWS_FT_FI9 |
Number of Residues | 40 |
Details | TRANSMEM: Helical; Name=7 => ECO:0000255 |
Chain | Residue | Details |
B | ILE525-ALA545 | |
A | ILE525-ALA545 |
site_id | SWS_FT_FI10 |
Number of Residues | 40 |
Details | TRANSMEM: Helical; Name=8 => ECO:0000255 |
Chain | Residue | Details |
B | PHE560-ILE580 | |
A | PHE560-ILE580 |
site_id | SWS_FT_FI11 |
Number of Residues | 40 |
Details | TRANSMEM: Helical; Name=9 => ECO:0000255 |
Chain | Residue | Details |
B | LEU586-ALA606 | |
A | LEU586-ALA606 |
site_id | SWS_FT_FI12 |
Number of Residues | 40 |
Details | TRANSMEM: Helical; Name=10 => ECO:0000255 |
Chain | Residue | Details |
B | VAL620-LEU640 | |
A | VAL620-LEU640 |
site_id | SWS_FT_FI13 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|PubMed:35917926, ECO:0007744|PDB:7XXB |
Chain | Residue | Details |
B | VAL51 | |
A | TYR145 | |
A | ILE600 | |
A | VAL601 | |
B | ASN112 | |
B | LEU114 | |
B | TYR145 | |
B | ILE600 | |
B | VAL601 | |
A | VAL51 | |
A | ASN112 | |
A | LEU114 |
site_id | SWS_FT_FI14 |
Number of Residues | 6 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9C6B8 |
Chain | Residue | Details |
B | SER226 | |
B | SER243 | |
B | SER283 | |
A | SER226 | |
A | SER243 | |
A | SER283 |
site_id | SWS_FT_FI15 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q9C6B8 |
Chain | Residue | Details |
B | THR322 | |
A | THR322 |
site_id | SWS_FT_FI16 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:19376835 |
Chain | Residue | Details |
B | SER366 | |
A | SER366 |