3RT0
Crystal structure of PYL10-HAB1 complex in the absence of abscisic acid (ABA)
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004722 | molecular_function | protein serine/threonine phosphatase activity |
A | 0006470 | biological_process | protein dephosphorylation |
A | 0043169 | molecular_function | cation binding |
B | 0004722 | molecular_function | protein serine/threonine phosphatase activity |
B | 0006470 | biological_process | protein dephosphorylation |
B | 0043169 | molecular_function | cation binding |
C | 0004864 | molecular_function | protein phosphatase inhibitor activity |
C | 0005515 | molecular_function | protein binding |
C | 0005634 | cellular_component | nucleus |
C | 0005737 | cellular_component | cytoplasm |
C | 0005886 | cellular_component | plasma membrane |
C | 0009738 | biological_process | abscisic acid-activated signaling pathway |
C | 0010427 | molecular_function | abscisic acid binding |
C | 0016020 | cellular_component | membrane |
C | 0038023 | molecular_function | signaling receptor activity |
C | 0042803 | molecular_function | protein homodimerization activity |
C | 0080163 | biological_process | regulation of protein serine/threonine phosphatase activity |
D | 0004864 | molecular_function | protein phosphatase inhibitor activity |
D | 0005515 | molecular_function | protein binding |
D | 0005634 | cellular_component | nucleus |
D | 0005737 | cellular_component | cytoplasm |
D | 0005886 | cellular_component | plasma membrane |
D | 0009738 | biological_process | abscisic acid-activated signaling pathway |
D | 0010427 | molecular_function | abscisic acid binding |
D | 0016020 | cellular_component | membrane |
D | 0038023 | molecular_function | signaling receptor activity |
D | 0042803 | molecular_function | protein homodimerization activity |
D | 0080163 | biological_process | regulation of protein serine/threonine phosphatase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 512 |
Chain | Residue |
A | ASP243 |
A | ASP432 |
A | ASP492 |
A | HOH544 |
A | HOH681 |
A | HOH727 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG B 512 |
Chain | Residue |
B | HOH673 |
B | HOH674 |
B | HOH675 |
B | ASP243 |
B | ASP432 |
B | ASP492 |
Functional Information from PROSITE/UniProt
site_id | PS01032 |
Number of Residues | 9 |
Details | PPM_1 PPM-type phosphatase domain signature. FFGVYDGHG |
Chain | Residue | Details |
A | PHE238-GLY246 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|Ref.10, ECO:0007744|PDB:3R6P |
Chain | Residue | Details |
C | LYS56 | |
D | LYS56 | |
A | ASP492 | |
B | ASP243 | |
B | ASP432 | |
B | ASP492 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:O49686 |
Chain | Residue | Details |
C | ALA85 | |
C | ARG112 | |
C | GLU137 | |
D | ALA85 | |
D | ARG112 | |
D | GLU137 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | SITE: Involved in ABA binding => ECO:0000250|UniProtKB:Q84MC7 |
Chain | Residue | Details |
C | PRO57 | |
C | ILE104 | |
C | VAL156 | |
C | LEU159 | |
D | PRO57 | |
D | ILE104 | |
D | VAL156 | |
D | LEU159 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | SITE: Involved in interactions with PP2Cs => ECO:0000250|UniProtKB:O49686 |
Chain | Residue | Details |
C | PRO84 | |
C | THR148 | |
D | PRO84 | |
D | THR148 |