eF-site ID 1toz_5-A PDB Code 1toz Model 5 Chain A click to enlarge Title NMR structure of the human NOTCH-1 ligand binding region Classification SIGNALING PROTEIN Compound Neurogenic locus notch homolog protein 1 Source Homo sapiens (Human) (NOTC1_HUMAN) Sequence A:  QDVDECSLGANPCEHAGKCINTLGSFECQCLQGYTGPRCE IDVNECVSNPCQNDATCLDQIGEFQCICMPGYEGVHCEVN TDECASSPCLHNGRCLDKINEFQCECPTGFTGHLCQ Description Functional site 1) chain A residue 429-440 type prosite sequence CINTLGSFECQC description ASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. CiNtlgsFeCqC source prosite : PS00010 2) chain A residue 467-478 type prosite sequence CLDQIGEFQCIC description ASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. CiNtlgsFeCqC source prosite : PS00010 3) chain A residue 505-516 type prosite sequence CLDKINEFQCEC description ASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. CiNtlgsFeCqC source prosite : PS00010 4) chain A residue 438-449 type prosite sequence CQCLQGYTGPRC description EGF_1 EGF-like domain signature 1. CqClqGytGPrC source prosite : PS00022 5) chain A residue 476-487 type prosite sequence CICMPGYEGVHC description EGF_1 EGF-like domain signature 1. CqClqGytGPrC source prosite : PS00022 6) chain A residue 514-525 type prosite sequence CECPTGFTGHLC description EGF_1 EGF-like domain signature 1. CqClqGytGPrC source prosite : PS00022 7) chain A residue 438-449 type prosite sequence CQCLQGYTGPRC description EGF_2 EGF-like domain signature 2. CqClqGYtgpr....C source prosite : PS01186 8) chain A residue 476-487 type prosite sequence CICMPGYEGVHC description EGF_2 EGF-like domain signature 2. CqClqGYtgpr....C source prosite : PS01186 9) chain A residue 514-525 type prosite sequence CECPTGFTGHLC description EGF_2 EGF-like domain signature 2. CqClqGYtgpr....C source prosite : PS01186 10) chain A residue 412-438 type prosite sequence DVDECSLGANPCEHAGKCINTLGSFEC description EGF_CA Calcium-binding EGF-like domain signature. DvDECslganp........Cehagk..CiNtlgsFeC source prosite : PS01187 11) chain A residue 452-476 type prosite sequence DVNECVSNPCQNDATCLDQIGEFQC description EGF_CA Calcium-binding EGF-like domain signature. DvDECslganp........Cehagk..CiNtlgsFeC source prosite : PS01187 12) chain A residue 490-514 type prosite sequence NTDECASSPCLHNGRCLDKINEFQC description EGF_CA Calcium-binding EGF-like domain signature. DvDECslganp........Cehagk..CiNtlgsFeC source prosite : PS01187 13) chain A residue 432 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:Q07008 source Swiss-Prot : SWS_FT_FI1 14) chain A residue 493 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:Q07008 source Swiss-Prot : SWS_FT_FI1 15) chain A residue 507 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:Q07008 source Swiss-Prot : SWS_FT_FI1 16) chain A residue 508 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:Q07008 source Swiss-Prot : SWS_FT_FI1 17) chain A residue 435 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:Q07008 source Swiss-Prot : SWS_FT_FI1 18) chain A residue 452 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:Q07008 source Swiss-Prot : SWS_FT_FI1 19) chain A residue 453 type BINDING sequence V description BINDING => ECO:0000250|UniProtKB:Q07008 source Swiss-Prot : SWS_FT_FI1 20) chain A residue 455 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:Q07008 source Swiss-Prot : SWS_FT_FI1 21) chain A residue 469 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:Q07008 source Swiss-Prot : SWS_FT_FI1 22) chain A residue 470 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:Q07008 source Swiss-Prot : SWS_FT_FI1 23) chain A residue 490 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:Q07008 source Swiss-Prot : SWS_FT_FI1 24) chain A residue 491 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:Q07008 source Swiss-Prot : SWS_FT_FI1 25) chain A residue 469 type SITE sequence D description Interaction with DLL4 => ECO:0000250|UniProtKB:Q07008 source Swiss-Prot : SWS_FT_FI2 26) chain A residue 435 type CARBOHYD sequence S description O-linked (Glc...) serine => ECO:0000269|PubMed:30127001 source Swiss-Prot : SWS_FT_FI3 27) chain A residue 458 type CARBOHYD sequence S description O-linked (Glc...) serine => ECO:0000250|UniProtKB:Q07008 source Swiss-Prot : SWS_FT_FI4 28) chain A residue 496 type CARBOHYD sequence S description O-linked (Glc...) serine => ECO:0000250|UniProtKB:Q07008 source Swiss-Prot : SWS_FT_FI4 29) chain A residue 466 type CARBOHYD sequence T description O-linked (Fuc...) threonine => ECO:0000250|UniProtKB:Q07008 source Swiss-Prot : SWS_FT_FI5

Display surface Download Links