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4D0F

Human Notch1 EGF domains 11-13 mutant T466A

Functional Information from GO Data
ChainGOidnamespacecontents
A0005509molecular_functioncalcium ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 1535
ChainResidue
AASP452
AVAL453
AGLU455
AASP469
AGLN470

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 1536
ChainResidue
ASER435
AVAL413
AGLU415
AASN431
ATHR432

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1537
ChainResidue
AASN490
ATHR491
AGLU493
AASP507
ALYS508
AHOH2005

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE EDO A 1538
ChainResidue
ACYS467

Functional Information from PROSITE/UniProt
site_idPS00010
Number of Residues12
DetailsASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. CiNtlgsFeCqC
ChainResidueDetails
ACYS429-CYS440
ACYS467-CYS478
ACYS505-CYS516

site_idPS00022
Number of Residues12
DetailsEGF_1 EGF-like domain signature 1. CqClqGytGPrC
ChainResidueDetails
ACYS438-CYS449
ACYS476-CYS487
ACYS514-CYS525

site_idPS01186
Number of Residues12
DetailsEGF_2 EGF-like domain signature 2. CqClqGYtgpr....C
ChainResidueDetails
ACYS438-CYS449
ACYS476-CYS487
ACYS514-CYS525

site_idPS01187
Number of Residues27
DetailsEGF_CA Calcium-binding EGF-like domain signature. DvDECslganp........Cehagk..CiNtlgsFeC
ChainResidueDetails
AASP412-CYS438
AASP452-CYS476
AASN490-CYS514

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues38
DetailsDomain: {"description":"EGF-like 11; calcium-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU00076","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues36
DetailsDomain: {"description":"EGF-like 12; calcium-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU00076","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues36
DetailsDomain: {"description":"EGF-like 13; calcium-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU00076","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues5
DetailsRegion: {"description":"Interaction with DLL4","evidences":[{"source":"UniProtKB","id":"Q07008","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q07008","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsSite: {"description":"Interaction with DLL4","evidences":[{"source":"UniProtKB","id":"Q07008","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsGlycosylation: {"description":"O-linked (Glc...) serine","evidences":[{"source":"PubMed","id":"30127001","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsGlycosylation: {"description":"O-linked (Glc...) serine","evidences":[{"source":"UniProtKB","id":"Q07008","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues1
DetailsGlycosylation: {"description":"O-linked (Fuc...) threonine","evidences":[{"source":"UniProtKB","id":"Q07008","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

246333

PDB entries from 2025-12-17

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