4WMQ
Structure of Human Intelectin-1
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0001934 | biological_process | positive regulation of protein phosphorylation |
| A | 0005509 | molecular_function | calcium ion binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005615 | cellular_component | extracellular space |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0009624 | biological_process | response to nematode |
| A | 0030246 | molecular_function | carbohydrate binding |
| A | 0031526 | cellular_component | brush border membrane |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0043235 | cellular_component | receptor complex |
| A | 0045121 | cellular_component | membrane raft |
| A | 0046326 | biological_process | positive regulation of D-glucose import |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 0070207 | biological_process | protein homotrimerization |
| A | 0070492 | molecular_function | oligosaccharide binding |
| A | 0098552 | cellular_component | side of membrane |
| B | 0001934 | biological_process | positive regulation of protein phosphorylation |
| B | 0005509 | molecular_function | calcium ion binding |
| B | 0005515 | molecular_function | protein binding |
| B | 0005576 | cellular_component | extracellular region |
| B | 0005615 | cellular_component | extracellular space |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0009624 | biological_process | response to nematode |
| B | 0030246 | molecular_function | carbohydrate binding |
| B | 0031526 | cellular_component | brush border membrane |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0043235 | cellular_component | receptor complex |
| B | 0045121 | cellular_component | membrane raft |
| B | 0046326 | biological_process | positive regulation of D-glucose import |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0070062 | cellular_component | extracellular exosome |
| B | 0070207 | biological_process | protein homotrimerization |
| B | 0070492 | molecular_function | oligosaccharide binding |
| B | 0098552 | cellular_component | side of membrane |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue CA A 401 |
| Chain | Residue |
| A | HIS86 |
| A | GLY97 |
| A | ASP133 |
| A | ASP282 |
| A | HOH589 |
| A | HOH663 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue CA A 402 |
| Chain | Residue |
| A | ASP98 |
| A | HOH573 |
| A | HOH640 |
| A | GLU87 |
| A | ASP89 |
| A | GLY92 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue CA A 403 |
| Chain | Residue |
| A | ASN260 |
| A | GLU262 |
| A | GLU274 |
| A | HOH534 |
| A | HOH611 |
| A | HOH619 |
| A | HOH632 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue CA B 401 |
| Chain | Residue |
| B | HIS86 |
| B | GLY97 |
| B | ASP133 |
| B | ASP282 |
| B | HOH563 |
| B | HOH632 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue CA B 402 |
| Chain | Residue |
| B | GLU87 |
| B | ASP89 |
| B | GLY92 |
| B | ASP98 |
| B | HOH581 |
| B | HOH582 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | binding site for residue CA B 403 |
| Chain | Residue |
| B | ASN260 |
| B | GLU262 |
| B | GLU274 |
| B | HOH534 |
| B | HOH558 |
| B | HOH578 |
| B | HOH605 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 28 |
| Details | Propeptide: {"featureId":"PRO_0000009144","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 223 |
| Details | Domain: {"description":"Fibrinogen C-terminal","evidences":[{"source":"PROSITE-ProRule","id":"PRU00739","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 22 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"26148048","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4WMQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4WMY","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"26148048","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4WMY","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Lipidation: {"description":"GPI-anchor amidated serine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
