2YMK
Crystal structure of the hexameric anti-microbial peptide channel dermcidin
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005576 | cellular_component | extracellular region |
| A | 0008233 | molecular_function | peptidase activity |
| A | 0031640 | biological_process | killing of cells of another organism |
| B | 0005576 | cellular_component | extracellular region |
| B | 0008233 | molecular_function | peptidase activity |
| B | 0031640 | biological_process | killing of cells of another organism |
| C | 0005576 | cellular_component | extracellular region |
| C | 0008233 | molecular_function | peptidase activity |
| C | 0031640 | biological_process | killing of cells of another organism |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 1049 |
| Chain | Residue |
| A | HIS38 |
| A | ASP42 |
| B | GLU5 |
| B | ASP9 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 1049 |
| Chain | Residue |
| A | GLU5 |
| A | ASP9 |
| B | HIS38 |
| B | ASP42 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN C 1049 |
| Chain | Residue |
| C | ASP9 |
| C | HIS38 |
| C | ASP42 |
| C | GLU5 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 1050 |
| Chain | Residue |
| A | ASP24 |
| A | ASP28 |
| A | HOH2003 |
| B | LYS6 |
| B | LYS20 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 1050 |
| Chain | Residue |
| B | ASP24 |
| B | ASP28 |
| B | HOH2002 |
| B | HOH2009 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ZN C 1050 |
| Chain | Residue |
| C | ASP24 |
| C | ASP28 |
| C | HOH2005 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | Propeptide: {"featureId":"PRO_0000408312","evidences":[{"source":"PubMed","id":"11694882","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25946035","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Binding site: {"description":"in chain A","evidences":[{"source":"PubMed","id":"23426625","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2YMK","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"23426625","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2YMK","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Binding site: {"description":"in chain B","evidences":[{"source":"PubMed","id":"23426625","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2YMK","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 88 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"23426625","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
