4N0G
Crystal Structure of PYL13-PP2CA complex
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 | 0038023 | molecular_function | signaling receptor activity |
| C | 0042803 | molecular_function | protein homodimerization 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 | 0038023 | molecular_function | signaling receptor activity |
| D | 0042803 | molecular_function | protein homodimerization activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 401 |
| Chain | Residue |
| A | CYS146 |
| A | HIS148 |
| A | CYS208 |
| A | CYS210 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 402 |
| Chain | Residue |
| A | GLU172 |
| A | GLU175 |
| A | HOH530 |
| D | GLU15 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG A 403 |
| Chain | Residue |
| A | ASP327 |
| A | ASP380 |
| A | MG404 |
| A | HOH502 |
| A | HOH503 |
| A | HOH590 |
| A | ASP142 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG A 404 |
| Chain | Residue |
| A | ASP142 |
| A | GLY143 |
| A | MG403 |
| A | HOH501 |
| A | HOH503 |
| A | HOH524 |
| A | HOH589 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 405 |
| Chain | Residue |
| A | ASP327 |
| A | ASP331 |
| A | HOH561 |
| A | HOH569 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 401 |
| Chain | Residue |
| B | CYS146 |
| B | HIS148 |
| B | CYS208 |
| B | CYS210 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 402 |
| Chain | Residue |
| B | ASP142 |
| B | ASP327 |
| B | ASP380 |
| B | MG403 |
| B | HOH502 |
| B | HOH503 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG B 403 |
| Chain | Residue |
| B | ASP142 |
| B | GLY143 |
| B | MG402 |
| B | HOH501 |
| B | HOH503 |
| B | HOH595 |
| B | HOH596 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG B 404 |
| Chain | Residue |
| B | GLU175 |
| C | GLU15 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG B 405 |
| Chain | Residue |
| B | ASP327 |
| B | ASP331 |
| B | HOH515 |
| B | HOH572 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG C 201 |
| Chain | Residue |
| B | HOH509 |
| C | ASP74 |
| C | HOH353 |
| C | HOH354 |
| C | HOH355 |
| site_id | BC3 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE MG D 201 |
| Chain | Residue |
| D | ASP74 |
Functional Information from PROSITE/UniProt
| site_id | PS01032 |
| Number of Residues | 9 |
| Details | PPM_1 PPM-type phosphatase domain signature. FYGVFDGHG |
| Chain | Residue | Details |
| A | PHE137-GLY145 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"24165892","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4N0G","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Site: {"description":"Lock","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | Motif: {"description":"Gate loop","evidences":[{"source":"UniProtKB","id":"Q8VZS8","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Motif: {"description":"Latch loop","evidences":[{"source":"UniProtKB","id":"Q8VZS8","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 24 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"O49686","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | Site: {"description":"Involved in interactions with PP2Cs","evidences":[{"source":"UniProtKB","id":"O49686","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Site: {"description":"Involved in ABA binding","evidences":[{"source":"UniProtKB","id":"Q84MC7","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
