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2VJ3

Human Notch-1 EGFs 11-13

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 1531
ChainResidue
AASP452
AVAL453
AGLU455
AASP469
AGLN470
AHOH2007
AHOH2009

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA A 1532
ChainResidue
AGLU415
AASN431
ATHR432
ASER435
AHOH2002
AASP412
AVAL413

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1533
ChainResidue
AASN490
ATHR491
AGLU493
AASP507
ALYS508
AHOH2015

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 1534
ChainResidue
AGLU511
AGLU511
AHIS523
AHIS523

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA A 1535
ChainResidue
ALEU524
ACYS525
AGLN526
ACL1537

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE NA A 1536
ChainResidue
AGLU483
AASP528

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 1537
ChainResidue
AGLU493
AASN510
ANA1535

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 1538
ChainResidue
AGLN475
ACYS476
AVAL485

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 Residues12
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q07008
ChainResidueDetails
ATHR432
AGLU493
AASP507
ALYS508
ASER435
AASP452
AVAL453
AGLU455
AASP469
AGLN470
AASN490
ATHR491

site_idSWS_FT_FI2
Number of Residues1
DetailsSITE: Interaction with DLL4 => ECO:0000250|UniProtKB:Q07008
ChainResidueDetails
AASP469

site_idSWS_FT_FI3
Number of Residues1
DetailsCARBOHYD: O-linked (Glc...) serine => ECO:0000269|PubMed:30127001
ChainResidueDetails
ASER435

site_idSWS_FT_FI4
Number of Residues2
DetailsCARBOHYD: O-linked (Glc...) serine => ECO:0000250|UniProtKB:Q07008
ChainResidueDetails
ASER458
ASER496

site_idSWS_FT_FI5
Number of Residues1
DetailsCARBOHYD: O-linked (Fuc...) threonine => ECO:0000250|UniProtKB:Q07008
ChainResidueDetails
ATHR466

217705

PDB entries from 2024-03-27

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