1EDM
EPIDERMAL GROWTH FACTOR-LIKE DOMAIN FROM HUMAN FACTOR IX
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA B 3 |
| Chain | Residue |
| B | SER53 |
| B | HOH204 |
| B | HOH208 |
| B | HOH209 |
| B | HOH210 |
| B | HOH234 |
| B | HOH254 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA C 1 |
| Chain | Residue |
| C | GLY48 |
| C | GLN50 |
| C | ASP64 |
| C | ASP65 |
| B | ASN58 |
| C | ASP47 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 2 |
| Chain | Residue |
| B | ASP47 |
| B | GLY48 |
| B | GLN50 |
| B | ASP64 |
| B | ASP65 |
| C | ASN58 |
Functional Information from PROSITE/UniProt
| site_id | PS00010 |
| Number of Residues | 12 |
| Details | ASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. CkDdinsYeCwC |
| Chain | Residue | Details |
| B | CYS62-CYS73 |
| site_id | PS00022 |
| Number of Residues | 12 |
| Details | EGF_1 EGF-like domain signature 1. CwCpfGfeGKnC |
| Chain | Residue | Details |
| B | CYS71-CYS82 |
| site_id | PS01186 |
| Number of Residues | 12 |
| Details | EGF_2 EGF-like domain signature 2. CwCpfGFegkn....C |
| Chain | Residue | Details |
| B | CYS71-CYS82 |
| site_id | PS01187 |
| Number of Residues | 25 |
| Details | EGF_CA Calcium-binding EGF-like domain signature. DgDQCesnp..........Clnggs..CkDdinsYeC |
| Chain | Residue | Details |
| B | ASP47-CYS71 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 72 |
| Details | Domain: {"description":"EGF-like 1; calcium-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU00076","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"7606779","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1EDM","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"(3R)-3-hydroxyaspartate","evidences":[{"source":"PubMed","id":"6688526","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"book","publicationDate":"1996","firstPage":"50","lastPage":"50","publisher":"Annecy","bookName":"Proceedings of XIth international conference on methods in protein structure analysis","title":"Partial phosphorylation of serine-68 in EGF-1 of human factor IX.","authors":["Harris R.J.","Papac D.I.","Truong L.","Smith K.J."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"O-linked (Glc...) serine","featureId":"CAR_000009","evidences":[{"source":"PubMed","id":"2129367","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2511201","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25456591","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"O-linked (Fuc...) serine","featureId":"CAR_000010","evidences":[{"source":"PubMed","id":"1517205","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25456591","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
