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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 401 |
| Chain | Residue |
| A | ASP118 |
| A | ASP306 |
| A | ASP368 |
| A | HOH505 |
| A | HOH509 |
| A | HOH520 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue MG A 402 |
| Chain | Residue |
| A | ASP306 |
| A | ASP310 |
| A | HOH516 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 403 |
| Chain | Residue |
| A | ASP118 |
| A | GLY119 |
| A | HOH502 |
| A | HOH503 |
| A | HOH520 |
| A | HOH530 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 401 |
| Chain | Residue |
| B | ASP118 |
| B | ASP306 |
| B | ASP368 |
| B | HOH511 |
| B | HOH513 |
| B | HOH524 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue MG B 402 |
| Chain | Residue |
| B | ASP306 |
| B | ASP310 |
| B | HOH509 |
| B | HOH520 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 403 |
| Chain | Residue |
| B | ASP118 |
| B | GLY119 |
| B | HOH504 |
| B | HOH513 |
| B | HOH514 |
| B | HOH526 |
| site_id | AC7 |
| Number of Residues | 10 |
| Details | binding site for residue A8S C 301 |
| Chain | Residue |
| C | LYS76 |
| C | VAL98 |
| C | ALA104 |
| C | PHE125 |
| C | PHE174 |
| C | LEU178 |
| C | ASN182 |
| C | HOH406 |
| C | HOH407 |
| C | HOH411 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue A8S D 301 |
| Chain | Residue |
| D | LYS76 |
| D | SER107 |
| D | PHE125 |
| D | HIS130 |
| D | LEU178 |
| D | ASN182 |
| D | HOH404 |
Functional Information from PROSITE/UniProt
| site_id | PS01032 |
| Number of Residues | 9 |
| Details | PPM_1 PPM-type phosphatase domain signature. LFGVFDGHG |
| Chain | Residue | Details |
| A | LEU113-GLY121 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Motif: {"description":"Modulates binding affinity to PYR/PYL/RCAR abscisic acid intracellular receptors","evidences":[{"source":"PubMed","id":"28827170","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 151 |
| Details | Region: {"description":"START-like","evidences":[{"source":"UniProtKB","id":"Q8H1R0","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | Motif: {"description":"Gate loop","evidences":[{"source":"UniProtKB","id":"Q8VZS8","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Motif: {"description":"Latch loop","evidences":[{"source":"UniProtKB","id":"Q8VZS8","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"28827170","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5GWP","evidenceCode":"ECO:0007744"}]} |
| site_id | SWS_FT_FI7 |
| Number of Residues | 24 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"O49686","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | Site: {"description":"Involved in ABA binding","evidences":[{"source":"UniProtKB","id":"Q84MC7","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI9 |
| Number of Residues | 4 |
| Details | Site: {"description":"Involved in interactions with PP2Cs","evidences":[{"source":"UniProtKB","id":"O49686","evidenceCode":"ECO:0000250"}]} |
