1G1Q
Crystal structure of P-selectin lectin/EGF domains
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 801 |
| Chain | Residue |
| A | GLU80 |
| A | ASN82 |
| A | ASN105 |
| A | ASP106 |
| A | HOH810 |
| A | HOH857 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 802 |
| Chain | Residue |
| B | ASP106 |
| B | HOH826 |
| B | HOH833 |
| B | GLU80 |
| B | ASN82 |
| B | ASN105 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA C 803 |
| Chain | Residue |
| C | GLU80 |
| C | ASN82 |
| C | ASN105 |
| C | ASP106 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA D 804 |
| Chain | Residue |
| D | GLU80 |
| D | ASN82 |
| D | ASN105 |
| D | ASP106 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MRD C 805 |
| Chain | Residue |
| C | THR2 |
| C | TYR3 |
| C | TYR37 |
| C | GLY138 |
| C | HOH814 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MRD A 806 |
| Chain | Residue |
| A | THR2 |
| A | TYR3 |
| A | TYR37 |
| A | ILE137 |
| A | GLY138 |
Functional Information from PROSITE/UniProt
| site_id | PS00022 |
| Number of Residues | 12 |
| Details | EGF_1 EGF-like domain signature 1. CsCypGfyGPeC |
| Chain | Residue | Details |
| A | CYS142-CYS153 |
| site_id | PS00615 |
| Number of Residues | 28 |
| Details | C_TYPE_LECTIN_1 C-type lectin domain signature. CVeiyikspsapgkWNDEHClkkkh.ALC |
| Chain | Residue | Details |
| A | CYS90-CYS117 |
| site_id | PS01186 |
| Number of Residues | 12 |
| Details | EGF_2 EGF-like domain signature 2. CsCypGFygpe....C |
| Chain | Residue | Details |
| A | CYS142-CYS153 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 400 |
| 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 | 144 |
| Details | Domain: {"description":"EGF-like","evidences":[{"source":"PROSITE-ProRule","id":"PRU00076","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11081633","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1G1Q","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1G1R","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"1G1R","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11081633","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1G1R","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16263699","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 8 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
