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5FM9

human Notch 1, EGF 4-7

Functional Information from GO Data
ChainGOidnamespacecontents
A0005509molecular_functioncalcium ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA A 1295
ChainResidue
AASP178
AVAL179
AGLU181
AASN197
AGLU198
ASER201
AHOH2001

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1296
ChainResidue
AASP260
AASP274
AGLY275
AHOH2006
AASN257
AILE258

Functional Information from PROSITE/UniProt
site_idPS00010
Number of Residues12
DetailsASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. ChNevgsYrCvC
ChainResidueDetails
ACYS195-CYS206
ACYS272-CYS283

site_idPS00022
Number of Residues12
DetailsEGF_1 EGF-like domain signature 1. ChCppSfhGPtC
ChainResidueDetails
ACYS164-CYS175
ACYS204-CYS215
ACYS243-CYS254
ACYS281-CYS292

site_idPS01186
Number of Residues12
DetailsEGF_2 EGF-like domain signature 2. CaClpGFtgqn....C
ChainResidueDetails
ACYS243-CYS254

site_idPS01187
Number of Residues27
DetailsEGF_CA Calcium-binding EGF-like domain signature. DvNECgqkpgl........Crhggt..ChNevgsYrC
ChainResidueDetails
AASP178-CYS204
AASN257-CYS281

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsCARBOHYD: O-linked (Glc...) serine => ECO:0000250|UniProtKB:Q01705
ChainResidueDetails
ASER146

site_idSWS_FT_FI2
Number of Residues1
DetailsCARBOHYD: O-linked (Fuc...) threonine => ECO:0000250|UniProtKB:Q01705
ChainResidueDetails
ATHR194

site_idSWS_FT_FI3
Number of Residues1
DetailsCARBOHYD: O-linked (GalNAc...) threonine; alternate => ECO:0000269|PubMed:24226769
ChainResidueDetails
ATHR232

220113

PDB entries from 2024-05-22

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