1HML
ALPHA_LACTALBUMIN POSSESSES A DISTINCT ZINC BINDING SITE
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA A 124 |
| Chain | Residue |
| A | ASP87 |
| A | ASP88 |
| A | HOH140 |
| A | HOH141 |
| A | LYS79 |
| A | ASP82 |
| A | ASP84 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 125 |
| Chain | Residue |
| A | GLU49 |
| A | GLU116 |
| A | HOH146 |
| A | HOH147 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 139 |
| Chain | Residue |
| A | GLN39 |
| A | ARG70 |
| A | LYS94 |
| A | HOH154 |
| A | HOH217 |
| site_id | CA |
| Number of Residues | 5 |
| Details |
| Chain | Residue |
| A | LYS79 |
| A | ASP82 |
| A | ASP84 |
| A | ASP87 |
| A | ASP88 |
| site_id | ZN |
| Number of Residues | 1 |
| Details |
| Chain | Residue |
| A | GLU49 |
Functional Information from PROSITE/UniProt
| site_id | PS00128 |
| Number of Residues | 19 |
| Details | GLYCOSYL_HYDROL_F22_1 Glycosyl hydrolases family 22 (GH22) domain signature. CdisCdkFlddDItddimC |
| Chain | Residue | Details |
| A | CYS73-CYS91 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 122 |
| Details | Domain: {"description":"C-type lysozyme","evidences":[{"source":"PROSITE-ProRule","id":"PRU00680","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"9537992","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1A4V","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"8366079","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1HML","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 5 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"8366079","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9537992","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1A4V","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1HML","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"18780401","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine; atypical; partial","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"1995","firstPage":"119","lastPage":"119","volume":"1","journal":"Protein Sci. 4 Suppl.","title":"An unusual glycosylation site in alpha-lactalbumin from human milk.","authors":["Cavaletto M.","Giuffrida M.G.","Giunta C.","Conti A."]}}]} |
| Chain | Residue | Details |
