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4L41

Human Lactose synthase: A 2:1 complex between human alpha-lactalbumin and human beta1,4-galactosyltransferase

Functional Information from GO Data
ChainGOidnamespacecontents
A0004461molecular_functionlactose synthase activity
A0005509molecular_functioncalcium ion binding
A0005989biological_processlactose biosynthetic process
B0004461molecular_functionlactose synthase activity
B0005509molecular_functioncalcium ion binding
B0005989biological_processlactose biosynthetic process
C0005975biological_processcarbohydrate metabolic process
C0016757molecular_functionglycosyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 201
ChainResidue
ALYS80
AASP83
AASP85
AASP88
AASP89
AHOH302

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 C 401
ChainResidue
CARG339
CARG342
CGLU144
CPHE145
CASN146

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 201
ChainResidue
BLYS80
BPHE81
BASP83
BASP85
BASP88
BASP89

Functional Information from PROSITE/UniProt
site_idPS00128
Number of Residues19
DetailsGLYCOSYL_HYDROL_F22_1 Glycosyl hydrolases family 22 (GH22) domain signature. CdisCdkFlddDItddimC
ChainResidueDetails
ACYS74-CYS92

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"9537992","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1A4V","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"8366079","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1HML","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues10
DetailsBinding 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"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"18780401","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsGlycosylation: {"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."]}}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues13
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"16497331","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"16157350","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19106107","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

244693

PDB entries from 2025-11-12

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