5B1W
Crystal structure of human dendritic cell inhibitory receptor (DCIR) C-type lectin domain in ligand-free form
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | binding site for residue CA A 2001 |
Chain | Residue |
A | VAL143 |
A | ASN145 |
A | GLU149 |
A | GLU231 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue CA A 2002 |
Chain | Residue |
A | HOH2101 |
A | GLU195 |
A | SER197 |
A | GLU201 |
A | ASN218 |
A | ASP219 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue CA B 2001 |
Chain | Residue |
B | VAL143 |
B | ASN145 |
B | GLU149 |
B | GLU231 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue CA B 2002 |
Chain | Residue |
B | GLU195 |
B | SER197 |
B | GLU201 |
B | ASN218 |
B | ASP219 |
B | HOH2101 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue CA C 2001 |
Chain | Residue |
C | VAL143 |
C | ASN145 |
C | GLU149 |
C | GLU231 |
site_id | AC6 |
Number of Residues | 6 |
Details | binding site for residue CA C 2002 |
Chain | Residue |
C | GLU195 |
C | SER197 |
C | GLU201 |
C | ASN218 |
C | ASP219 |
C | HOH2101 |
site_id | AC7 |
Number of Residues | 4 |
Details | binding site for residue CA D 2001 |
Chain | Residue |
D | VAL143 |
D | ASN145 |
D | GLU149 |
D | GLU231 |
site_id | AC8 |
Number of Residues | 6 |
Details | binding site for residue CA D 2002 |
Chain | Residue |
D | GLU195 |
D | SER197 |
D | GLU201 |
D | ASN218 |
D | ASP219 |
D | HOH2101 |
Functional Information from PROSITE/UniProt
site_id | PS00615 |
Number of Residues | 28 |
Details | C_TYPE_LECTIN_1 C-type lectin domain signature. CVvlnfrkspkrwgWNDVNClgpqr.SVC |
Chain | Residue | Details |
A | CYS203-CYS230 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 472 |
Details | Domain: {"description":"C-type lectin","evidences":[{"source":"PROSITE-ProRule","id":"PRU00040","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 36 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"27015765","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5B1W","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5B1X","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 16 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"27015765","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5B1X","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |