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5AO6

Endo180 D1-4, trigonal form

Functional Information from PROSITE/UniProt
site_idPS00023
Number of Residues42
DetailsFN2_1 Fibronectin type-II collagen-binding domain signature. CtiPFkYdnqwfhgCtstgredghlWCattqDYgkderWgFC
ChainResidueDetails
ACYS187-CYS228

site_idPS00615
Number of Residues25
DetailsC_TYPE_LECTIN_1 C-type lectin domain signature. CGvirtessgg...WQNRDCsialp.YVC
ChainResidueDetails
ACYS335-CYS359
ACYS481-CYS504

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues96
DetailsDomain: {"description":"Fibronectin type-II","evidences":[{"source":"PROSITE-ProRule","id":"PRU00479","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues232
DetailsDomain: {"description":"C-type lectin 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00040","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues232
DetailsDomain: {"description":"C-type lectin 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00040","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"19139490","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

239492

PDB entries from 2025-07-30

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