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2RR2

Structure of O-fucosylated epidermal growth factor-like repeat 12 of mouse Notch-1 receptor

Functional Information from GO Data
ChainGOidnamespacecontents
A0005509molecular_functioncalcium ion binding
Functional Information from PROSITE/UniProt
site_idPS00010
Number of Residues12
DetailsASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. ClDqigeFqCiC
ChainResidueDetails
ACYS16-CYS27

site_idPS00022
Number of Residues12
DetailsEGF_1 EGF-like domain signature 1. CiCmpGyeGVyC
ChainResidueDetails
ACYS25-CYS36

site_idPS01186
Number of Residues12
DetailsEGF_2 EGF-like domain signature 2. CiCmpGYegvy....C
ChainResidueDetails
ACYS25-CYS36

site_idPS01187
Number of Residues25
DetailsEGF_CA Calcium-binding EGF-like domain signature. DvNECisnp..........Cqndat..ClDqigeFqC
ChainResidueDetails
AASP1-CYS25

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q07008
ChainResidueDetails
AASP1
AVAL2
AGLU4
AASP18
AGLN19

site_idSWS_FT_FI2
Number of Residues1
DetailsSITE: Interaction with DLL4 => ECO:0000250|UniProtKB:Q07008
ChainResidueDetails
AASP18

site_idSWS_FT_FI3
Number of Residues1
DetailsCARBOHYD: O-linked (Glc...) serine => ECO:0000269|PubMed:21757702, ECO:0000269|PubMed:28089369
ChainResidueDetails
ASER7

site_idSWS_FT_FI4
Number of Residues1
DetailsCARBOHYD: O-linked (Fuc...) threonine => ECO:0000269|PubMed:21757702, ECO:0000269|PubMed:28089369
ChainResidueDetails
ATHR15

237735

PDB entries from 2025-06-18

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