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7EKA

crystal structure of epigallocatechin binding with alpha-lactalbumin

Functional Information from GO Data
ChainGOidnamespacecontents
A0003796molecular_functionlysozyme activity
A0004461molecular_functionlactose synthase activity
A0005509molecular_functioncalcium ion binding
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005989biological_processlactose biosynthetic process
A0032355biological_processresponse to estradiol
A0032570biological_processresponse to progesterone
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
A0050829biological_processdefense response to Gram-negative bacterium
A0050830biological_processdefense response to Gram-positive bacterium
A1903494biological_processresponse to dehydroepiandrosterone
A1903496biological_processresponse to 11-deoxycorticosterone
Functional Information from PROSITE/UniProt
site_idPS00128
Number of Residues19
DetailsGLYCOSYL_HYDROL_F22_1 Glycosyl hydrolases family 22 (GH22) domain signature. CnisCdkFlddDLtddimC
ChainResidueDetails
ACYS73-CYS91

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"8805552","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1HFZ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

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