4OIC
Crystal structrual of a soluble protein
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004864 | molecular_function | protein phosphatase inhibitor activity |
A | 0005515 | molecular_function | protein binding |
A | 0005634 | cellular_component | nucleus |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0009409 | biological_process | response to cold |
A | 0009414 | biological_process | response to water deprivation |
A | 0009738 | biological_process | abscisic acid-activated signaling pathway |
A | 0009845 | biological_process | seed germination |
A | 0010427 | molecular_function | abscisic acid binding |
A | 0038023 | molecular_function | signaling receptor activity |
A | 0042803 | molecular_function | protein homodimerization activity |
A | 1905183 | biological_process | negative regulation of protein serine/threonine phosphatase activity |
B | 0004721 | molecular_function | phosphoprotein phosphatase activity |
B | 0004722 | molecular_function | protein serine/threonine phosphatase activity |
B | 0005515 | molecular_function | protein binding |
B | 0005634 | cellular_component | nucleus |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0006470 | biological_process | protein dephosphorylation |
B | 0009738 | biological_process | abscisic acid-activated signaling pathway |
B | 0017018 | molecular_function | myosin phosphatase activity |
B | 0043169 | molecular_function | cation binding |
B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE A8S A 301 |
Chain | Residue |
A | LYS74 |
A | HOH415 |
A | HOH423 |
A | HOH426 |
A | HOH428 |
A | PHE76 |
A | ALA104 |
A | SER107 |
A | PHE123 |
A | TYR135 |
A | PHE180 |
A | ASN188 |
A | HOH401 |
site_id | AC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL A 302 |
Chain | Residue |
A | ARG78 |
B | GLU161 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MN B 501 |
Chain | Residue |
B | ASP205 |
B | ASP386 |
B | ASP448 |
B | HOH603 |
B | HOH605 |
B | HOH640 |
B | HOH647 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN B 502 |
Chain | Residue |
B | ASP205 |
B | GLY206 |
B | HOH601 |
B | HOH602 |
B | HOH603 |
B | HOH604 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN B 503 |
Chain | Residue |
B | ASP386 |
B | ASP390 |
B | HOH606 |
B | HOH607 |
B | HOH608 |
B | HOH675 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN B 504 |
Chain | Residue |
B | ASP324 |
B | ASP324 |
B | HOH614 |
B | HOH614 |
B | HOH615 |
B | HOH615 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE NA B 505 |
Chain | Residue |
B | ARG322 |
B | ARG322 |
B | GLU323 |
B | GLU323 |
Functional Information from PROSITE/UniProt
site_id | PS01032 |
Number of Residues | 9 |
Details | PPM_1 PPM-type phosphatase domain signature. FFGVYDGHG |
Chain | Residue | Details |
B | PHE200-GLY208 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
B | ASP205 | |
B | GLY206 | |
B | ASP386 | |
B | ASP448 |
site_id | SWS_FT_FI2 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:O49686 |
Chain | Residue | Details |
A | ALA104 | |
A | ARG131 | |
A | GLU162 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | SITE: Involved in interactions with PP2Cs => ECO:0000250|UniProtKB:O49686 |
Chain | Residue | Details |
A | PRO103 | |
A | THR173 |