3KLX
Crystal structure of native abscisic acid receptor PYL3
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 | 0009738 | biological_process | abscisic acid-activated signaling pathway |
| A | 0010427 | molecular_function | abscisic acid binding |
| A | 0038023 | molecular_function | signaling receptor activity |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| B | 0004864 | molecular_function | protein phosphatase inhibitor activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005634 | cellular_component | nucleus |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0009738 | biological_process | abscisic acid-activated signaling pathway |
| B | 0010427 | molecular_function | abscisic acid binding |
| B | 0038023 | molecular_function | signaling receptor activity |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0042803 | molecular_function | protein homodimerization activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 300 |
| Chain | Residue |
| A | PHE81 |
| A | VAL108 |
| A | PHE188 |
| A | VAL192 |
| A | HOH227 |
| A | HOH253 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 B 300 |
| Chain | Residue |
| B | VAL108 |
| B | SER109 |
| B | PHE188 |
| B | HOH241 |
| A | PHE188 |
| A | HOH253 |
| B | PHE81 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Motif: {"description":"Gate loop","evidences":[{"source":"UniProtKB","id":"Q8VZS8","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Motif: {"description":"Latch loop","evidences":[{"source":"UniProtKB","id":"Q8VZS8","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22579247","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23844015","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4DS8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4DSB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4DSC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4JDA","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"O49686","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22579247","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4DSC","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| 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_FI7 |
| Number of Residues | 2 |
| Details | Site: {"description":"Involved in ABA binding","evidences":[{"source":"UniProtKB","id":"Q84MC7","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Site: {"description":"Involved in the cis- to trans-homodimer conformation in the presence of ABA","evidences":[{"source":"PubMed","id":"22579247","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
