9LUM
Cryo-EM structure of Arabidopsis thaliana RGA in complex with GID1A
Functional Information from PROSITE/UniProt
site_id | PS01173 |
Number of Residues | 17 |
Details | LIPASE_GDXG_HIS Lipolytic enzymes "G-D-X-G" family, putative histidine active site. ILfFHGGSFahsSanSA |
Chain | Residue | Details |
B | ILE109-ALA125 |
site_id | PS01174 |
Number of Residues | 13 |
Details | LIPASE_GDXG_SER Lipolytic enzymes "G-D-X-G" family, putative serine active site. IfLAGDSSGGnIA |
Chain | Residue | Details |
B | ILE185-ALA197 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 54 |
Details | Region: {"description":"Leucine repeat I (LRI)","evidences":[{"source":"PROSITE-ProRule","id":"PRU01191","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 65 |
Details | Region: {"description":"VHIID","evidences":[{"source":"PROSITE-ProRule","id":"PRU01191","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 32 |
Details | Region: {"description":"Leucine repeat II (LRII)","evidences":[{"source":"PROSITE-ProRule","id":"PRU01191","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 87 |
Details | Region: {"description":"PFYRE","evidences":[{"source":"PROSITE-ProRule","id":"PRU01191","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 76 |
Details | Region: {"description":"SAW","evidences":[{"source":"PROSITE-ProRule","id":"PRU01191","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | Motif: {"description":"DELLA motif"} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 4 |
Details | Motif: {"description":"LEXLE motif"} |
Chain | Residue | Details |
site_id | SWS_FT_FI8 |
Number of Residues | 4 |
Details | Motif: {"description":"VHYNP motif"} |
Chain | Residue | Details |
site_id | SWS_FT_FI9 |
Number of Residues | 4 |
Details | Motif: {"description":"VHIID","evidences":[{"source":"PROSITE-ProRule","id":"PRU01191","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI10 |
Number of Residues | 4 |
Details | Motif: {"description":"LXXLL motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01191","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI11 |
Number of Residues | 2 |
Details | Motif: {"description":"Involved in the stabilization of the negatively charged intermediate by the formation of the oxyanion hole","evidences":[{"source":"UniProtKB","id":"Q5NUF3","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI12 |
Number of Residues | 2 |
Details | Active site: {"evidences":[{"source":"UniProtKB","id":"Q0ZPV7","evidenceCode":"ECO:0000250"},{"source":"PROSITE-ProRule","id":"PRU10038","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI13 |
Number of Residues | 4 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"19037309","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2ZSI","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI14 |
Number of Residues | 2 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"19037309","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2ZSH","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |