6POL
Crystal structure of the human NELL1 EGF1-3-Robo3 FN1 complex
Functional Information from GO Data
Functional Information from PROSITE/UniProt
site_id | PS00010 |
Number of Residues | 12 |
Details | ASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. CvNlpglYrCdC |
Chain | Residue | Details |
B | CYS451-CYS462 |
site_id | PS01186 |
Number of Residues | 15 |
Details | EGF_2 EGF-like domain signature 2. CdCvpGYirvddfs.C |
Chain | Residue | Details |
B | CYS460-CYS474 | |
B | CYS502-CYS515 |
site_id | PS01187 |
Number of Residues | 27 |
Details | EGF_CA Calcium-binding EGF-like domain signature. DiDECaakmhy........Chantv..CvNlpglYrC |
Chain | Residue | Details |
B | ASP434-CYS460 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 282 |
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 | 123 |
Details | Domain: {"description":"EGF-like 1; calcium-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU00076","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 120 |
Details | Domain: {"description":"EGF-like 2; calcium-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU00076","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 18 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"32198364","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6POL","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 3 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"32198364","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6POL","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |