8AVD
Cryo-EM structure for a 3:3 complex between mouse leptin and the mouse LEP-R ectodomain (local refinement)
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005179 | molecular_function | hormone activity |
A | 0005576 | cellular_component | extracellular region |
A | 0007165 | biological_process | signal transduction |
B | 0003700 | molecular_function | DNA-binding transcription factor activity |
B | 0004896 | molecular_function | cytokine receptor activity |
B | 0006355 | biological_process | regulation of DNA-templated transcription |
B | 0016020 | cellular_component | membrane |
C | 0005179 | molecular_function | hormone activity |
C | 0005576 | cellular_component | extracellular region |
C | 0007165 | biological_process | signal transduction |
D | 0003700 | molecular_function | DNA-binding transcription factor activity |
D | 0004896 | molecular_function | cytokine receptor activity |
D | 0006355 | biological_process | regulation of DNA-templated transcription |
D | 0016020 | cellular_component | membrane |
E | 0005179 | molecular_function | hormone activity |
E | 0005576 | cellular_component | extracellular region |
E | 0007165 | biological_process | signal transduction |
F | 0003700 | molecular_function | DNA-binding transcription factor activity |
F | 0004896 | molecular_function | cytokine receptor activity |
F | 0006355 | biological_process | regulation of DNA-templated transcription |
F | 0016020 | cellular_component | membrane |
Functional Information from PROSITE/UniProt
site_id | PS01353 |
Number of Residues | 57 |
Details | HEMATOPO_REC_L_F2 Long hematopoietin receptor, gp130 family signature. NslgaSlvnfnltfswpmskvsaveslsayplssscvi...LsWtlsPddysll...YlvIeW |
Chain | Residue | Details |
B | ASN716-TRP772 |
site_id | PS01355 |
Number of Residues | 31 |
Details | HEMATOPO_REC_S_F1 Short hematopoietin receptor family 1 signature. VlpgssyevqVRskrldgsgv...........WSdWSspqvF |
Chain | Residue | Details |
B | VAL296-PHE326 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 279 |
Details | Domain: {"description":"Fibronectin type-III 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00316","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 294 |
Details | Domain: {"description":"Ig-like"} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 285 |
Details | Domain: {"description":"Fibronectin type-III 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00316","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 51 |
Details | Region: {"description":"Leptin-binding","evidences":[{"source":"UniProtKB","id":"P48357","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 12 |
Details | Motif: {"description":"WSXWS motif"} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 15 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |