6POG
Crystal structure of the NELL2 EGF1-6-Robo3 FN1 complex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| B | 0005509 | molecular_function | calcium ion binding |
Functional Information from PROSITE/UniProt
| site_id | PS00010 |
| Number of Residues | 12 |
| Details | ASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. CvNtpgsFmCiC |
| Chain | Residue | Details |
| B | CYS457-CYS468 | |
| B | CYS572-CYS583 | |
| B | CYS619-CYS630 |
| site_id | PS00022 |
| Number of Residues | 12 |
| Details | EGF_1 EGF-like domain signature 1. CaCpqGftGPsC |
| Chain | Residue | Details |
| B | CYS541-CYS552 |
| site_id | PS01186 |
| Number of Residues | 15 |
| Details | EGF_2 EGF-like domain signature 2. CiCktGYiriddys.C |
| Chain | Residue | Details |
| B | CYS466-CYS480 | |
| B | CYS508-CYS521 | |
| B | CYS541-CYS552 |
| site_id | PS01187 |
| Number of Residues | 27 |
| Details | EGF_CA Calcium-binding EGF-like domain signature. DiDECaegrhy........Crentm..CvNtpgsFmC |
| Chain | Residue | Details |
| B | ASP440-CYS466 | |
| B | ASP555-CYS581 | |
| B | ASP602-CYS628 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 94 |
| 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 | 41 |
| Details | Domain: {"description":"EGF-like 2; calcium-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU00076","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 40 |
| Details | Domain: {"description":"EGF-like 3; calcium-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU00076","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 30 |
| Details | Domain: {"description":"EGF-like 4","evidences":[{"source":"PROSITE-ProRule","id":"PRU00076","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 46 |
| Details | Domain: {"description":"EGF-like 5; calcium-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU00076","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 18 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"32198364","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6POG","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"32198364","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6POG","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"O-linked (GlcNAc...) threonine","evidences":[{"source":"PubMed","id":"32198364","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6POG","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
