3KDJ
Complex structure of (+)-ABA-bound PYL1 and ABI1
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 | 0005886 | cellular_component | plasma membrane |
| A | 0006952 | biological_process | defense response |
| A | 0009536 | cellular_component | plastid |
| A | 0009738 | biological_process | abscisic acid-activated signaling pathway |
| A | 0010427 | molecular_function | abscisic acid binding |
| A | 0019888 | molecular_function | protein phosphatase regulator activity |
| A | 0038023 | molecular_function | signaling receptor activity |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0062049 | cellular_component | protein phosphatase inhibitor complex |
| 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 | 16 |
| Details | BINDING SITE FOR RESIDUE A8S A 222 |
| Chain | Residue |
| A | LYS86 |
| A | VAL193 |
| A | ASN197 |
| A | HOH223 |
| A | HOH228 |
| A | HOH230 |
| A | HOH250 |
| A | HOH257 |
| A | PHE88 |
| A | VAL110 |
| A | ALA116 |
| A | PHE135 |
| A | ILE137 |
| A | LEU144 |
| A | TYR147 |
| A | PHE189 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN B 435 |
| Chain | Residue |
| B | ASP177 |
| B | ASP347 |
| B | ASP413 |
| B | HOH466 |
| B | HOH488 |
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 | PHE172-GLY180 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 156 |
| Details | Region: {"description":"START-like"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Motif: {"description":"Gate loop","evidences":[{"source":"PubMed","id":"19898420","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Motif: {"description":"Latch loop","evidences":[{"source":"PubMed","id":"19898420","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 13 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"19855379","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19893533","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Site: {"description":"Involved in interactions with PP2Cs","evidences":[{"source":"PubMed","id":"19855379","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Site: {"description":"Involved in interactions with PP2Cs","evidences":[{"source":"UniProtKB","id":"O49686","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 5 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"3NMN","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Site: {"description":"Lock","evidences":[{"source":"UniProtKB","id":"Q9CAJ0","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
