eF-site ID 2vj3-A PDB Code 2vj3 Chain A click to enlarge Title Human Notch-1 EGFs 11-13 Classification TRANSCRIPTION Compound NEUROGENIC LOCUS NOTCH HOMOLOG PROTEIN 1 Source (NOTC1_HUMAN) Sequence A:  QDVDECSLGANPCEHAGKCINTLGSFECQCLQGYTGPRCE IDVNECVSNPCQNDATCLDQIGEFQCICMPGYEGVHCEVN TDECASSPCLHNGRCLDKINEFQCECPTGFTGHLCQVDLH Description Functional site 1) chain A residue 452 type sequence D description BINDING SITE FOR RESIDUE CA A 1531 source : AC1 2) chain A residue 453 type sequence V description BINDING SITE FOR RESIDUE CA A 1531 source : AC1 3) chain A residue 455 type sequence E description BINDING SITE FOR RESIDUE CA A 1531 source : AC1 4) chain A residue 469 type sequence D description BINDING SITE FOR RESIDUE CA A 1531 source : AC1 5) chain A residue 470 type sequence Q description BINDING SITE FOR RESIDUE CA A 1531 source : AC1 6) chain A residue 412 type sequence D description BINDING SITE FOR RESIDUE CA A 1532 source : AC2 7) chain A residue 413 type sequence V description BINDING SITE FOR RESIDUE CA A 1532 source : AC2 8) chain A residue 415 type sequence E description BINDING SITE FOR RESIDUE CA A 1532 source : AC2 9) chain A residue 431 type sequence N description BINDING SITE FOR RESIDUE CA A 1532 source : AC2 10) chain A residue 432 type sequence T description BINDING SITE FOR RESIDUE CA A 1532 source : AC2 11) chain A residue 435 type sequence S description BINDING SITE FOR RESIDUE CA A 1532 source : AC2 12) chain A residue 490 type sequence N description BINDING SITE FOR RESIDUE CA A 1533 source : AC3 13) chain A residue 491 type sequence T description BINDING SITE FOR RESIDUE CA A 1533 source : AC3 14) chain A residue 493 type sequence E description BINDING SITE FOR RESIDUE CA A 1533 source : AC3 15) chain A residue 507 type sequence D description BINDING SITE FOR RESIDUE CA A 1533 source : AC3 16) chain A residue 508 type sequence K description BINDING SITE FOR RESIDUE CA A 1533 source : AC3 17) chain A residue 511 type sequence E description BINDING SITE FOR RESIDUE CA A 1534 source : AC4 18) chain A residue 511 type sequence E description BINDING SITE FOR RESIDUE CA A 1534 source : AC4 19) chain A residue 523 type sequence H description BINDING SITE FOR RESIDUE CA A 1534 source : AC4 20) chain A residue 523 type sequence H description BINDING SITE FOR RESIDUE CA A 1534 source : AC4 21) chain A residue 524 type sequence L description BINDING SITE FOR RESIDUE NA A 1535 source : AC5 22) chain A residue 525 type sequence C description BINDING SITE FOR RESIDUE NA A 1535 source : AC5 23) chain A residue 526 type sequence Q description BINDING SITE FOR RESIDUE NA A 1535 source : AC5 24) chain A residue 483 type sequence E description BINDING SITE FOR RESIDUE NA A 1536 source : AC6 25) chain A residue 528 type sequence D description BINDING SITE FOR RESIDUE NA A 1536 source : AC6 26) chain A residue 493 type sequence E description BINDING SITE FOR RESIDUE CL A 1537 source : AC7 27) chain A residue 510 type sequence N description BINDING SITE FOR RESIDUE CL A 1537 source : AC7 28) chain A residue 475 type sequence Q description BINDING SITE FOR RESIDUE CL A 1538 source : AC8 29) chain A residue 476 type sequence C description BINDING SITE FOR RESIDUE CL A 1538 source : AC8 30) chain A residue 485 type sequence V description BINDING SITE FOR RESIDUE CL A 1538 source : AC8 31) chain A residue 429-440 type prosite sequence CINTLGSFECQC description ASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. CiNtlgsFeCqC source prosite : PS00010 32) chain A residue 467-478 type prosite sequence CLDQIGEFQCIC description ASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. CiNtlgsFeCqC source prosite : PS00010 33) chain A residue 505-516 type prosite sequence CLDKINEFQCEC description ASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. CiNtlgsFeCqC source prosite : PS00010 34) chain A residue 438-449 type prosite sequence CQCLQGYTGPRC description EGF_1 EGF-like domain signature 1. CqClqGytGPrC source prosite : PS00022 35) chain A residue 476-487 type prosite sequence CICMPGYEGVHC description EGF_1 EGF-like domain signature 1. CqClqGytGPrC source prosite : PS00022 36) chain A residue 514-525 type prosite sequence CECPTGFTGHLC description EGF_1 EGF-like domain signature 1. CqClqGytGPrC source prosite : PS00022 37) chain A residue 438-449 type prosite sequence CQCLQGYTGPRC description EGF_2 EGF-like domain signature 2. CqClqGYtgpr....C source prosite : PS01186 38) chain A residue 476-487 type prosite sequence CICMPGYEGVHC description EGF_2 EGF-like domain signature 2. CqClqGYtgpr....C source prosite : PS01186 39) chain A residue 514-525 type prosite sequence CECPTGFTGHLC description EGF_2 EGF-like domain signature 2. CqClqGYtgpr....C source prosite : PS01186 40) chain A residue 412-438 type prosite sequence DVDECSLGANPCEHAGKCINTLGSFEC description EGF_CA Calcium-binding EGF-like domain signature. DvDECslganp........Cehagk..CiNtlgsFeC source prosite : PS01187 41) chain A residue 452-476 type prosite sequence DVNECVSNPCQNDATCLDQIGEFQC description EGF_CA Calcium-binding EGF-like domain signature. DvDECslganp........Cehagk..CiNtlgsFeC source prosite : PS01187 42) chain A residue 490-514 type prosite sequence NTDECASSPCLHNGRCLDKINEFQC description EGF_CA Calcium-binding EGF-like domain signature. DvDECslganp........Cehagk..CiNtlgsFeC source prosite : PS01187 43) chain A residue 435 type CARBOHYD sequence S description O-linked (Glc...) serine => ECO:0000269|PubMed:30127001 source Swiss-Prot : SWS_FT_FI3 44) chain A residue 458 type CARBOHYD sequence S description O-linked (Glc...) serine => ECO:0000250|UniProtKB:Q07008 source Swiss-Prot : SWS_FT_FI4 45) chain A residue 496 type CARBOHYD sequence S description O-linked (Glc...) serine => ECO:0000250|UniProtKB:Q07008 source Swiss-Prot : SWS_FT_FI4 46) chain A residue 466 type CARBOHYD sequence T description O-linked (Fuc...) threonine => ECO:0000250|UniProtKB:Q07008 source Swiss-Prot : SWS_FT_FI5 47) chain A residue 432 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:Q07008 source Swiss-Prot : SWS_FT_FI1 48) chain A residue 493 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:Q07008 source Swiss-Prot : SWS_FT_FI1 49) chain A residue 507 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:Q07008 source Swiss-Prot : SWS_FT_FI1 50) chain A residue 508 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:Q07008 source Swiss-Prot : SWS_FT_FI1 51) chain A residue 435 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:Q07008 source Swiss-Prot : SWS_FT_FI1 52) chain A residue 452 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:Q07008 source Swiss-Prot : SWS_FT_FI1 53) chain A residue 453 type BINDING sequence V description BINDING => ECO:0000250|UniProtKB:Q07008 source Swiss-Prot : SWS_FT_FI1 54) chain A residue 455 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:Q07008 source Swiss-Prot : SWS_FT_FI1 55) chain A residue 469 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:Q07008 source Swiss-Prot : SWS_FT_FI1 56) chain A residue 470 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:Q07008 source Swiss-Prot : SWS_FT_FI1 57) chain A residue 490 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:Q07008 source Swiss-Prot : SWS_FT_FI1 58) chain A residue 491 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:Q07008 source Swiss-Prot : SWS_FT_FI1 59) chain A residue 469 type SITE sequence D description Interaction with DLL4 => ECO:0000250|UniProtKB:Q07008 source Swiss-Prot : SWS_FT_FI2

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