eF-site ID 6ha7-ABCD PDB Code 6ha7 Chain A, B, C, D click to enlarge Title Crystal structure of the BiP NBD and MANF complex Classification CHAPERONE Compound Endoplasmic reticulum chaperone BiP Source (MANF_MOUSE) Sequence A:  SGTVVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYV AFTPEGERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDP SVQQDIKFLPFKVVEKKTKPYIQVDIGGGQTKTFAPEEIS AMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKD AGTIAGLNVMRIINEPTAAAIAYGLDKREGEKNILVFDLG GGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHF IKLYKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQAR IEIESFFEGEDFSETLTRAKFEELNMDLFRSTMKPVQKVL EDSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFNGKEPSR GINPDEAVAYGAAVQAGVLS B:  SGTVVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYV AFTPEGERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDP SVQQDIKFLPFKVVEKKTKPYIQVDIGGGQTKTFAPEEIS AMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKD AGTIAGLNVMRIINEPTAAAIAYGLDKREGEKNILVFDLG GGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHF IKLYKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQAR IEIESFFEGEDFSETLTRAKFEELNMDLFRSTMKPVQKVL EDSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFNGKEPSR GINPDEAVAYGAAVQAGVLSG C:  RPGDCEVCISYLGRFYQDLKDRDVTFSPATIEEELIKFCR EARGKENRLCYYIGATKIINEVSKPLAHHIPVEKICEKLK KKDSQICELKYDNQIDLSTVDLKKLRVKELKKILDDWGEM CKGCAEKSDYIRKINELMPKYAPKAASARTDL D:  LRPGDCEVCISYLGRFYQDLKDRDVTFSPATIEEELIKFC REARGKENRLCYYIGATAATKIINEVSKPLAHHIPVEKIC EKLKKKDSQICELKYDNQIDLSTVDLKKLRVKELKKILDD WGEMCKGCAEKSDYIRKINELMPKYAPKAASAR Description Functional site 1) chain A residue 34 type sequence D description binding site for residue EDO A 501 source : AC1 2) chain A residue 36 type sequence G description binding site for residue EDO A 501 source : AC1 3) chain A residue 394 type sequence V description binding site for residue EDO A 501 source : AC1 4) chain B residue 34 type sequence D description binding site for residue EDO B 501 source : AC2 5) chain B residue 36 type sequence G description binding site for residue EDO B 501 source : AC2 6) chain A residue 353 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate => ECO:0000250|UniProtKB:P11021 source Swiss-Prot : SWS_FT_FI9 7) chain B residue 353 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate => ECO:0000250|UniProtKB:P11021 source Swiss-Prot : SWS_FT_FI9 8) chain A residue 96 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P11021 source Swiss-Prot : SWS_FT_FI2 9) chain B residue 96 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P11021 source Swiss-Prot : SWS_FT_FI2 10) chain C residue 73 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:18034455 source Swiss-Prot : SWS_FT_FI1 11) chain D residue 73 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:18034455 source Swiss-Prot : SWS_FT_FI1 12) chain A residue 293 type MOD_RES sequence E description Phosphotyrosine => ECO:0007744|PubMed:18034455 source Swiss-Prot : SWS_FT_FI1 13) chain A residue 364 type MOD_RES sequence G description Phosphotyrosine => ECO:0007744|PubMed:18034455 source Swiss-Prot : SWS_FT_FI1 14) chain B residue 36 type MOD_RES sequence G description Phosphotyrosine => ECO:0007744|PubMed:18034455 source Swiss-Prot : SWS_FT_FI1 15) chain B residue 227 type MOD_RES sequence G description Phosphotyrosine => ECO:0007744|PubMed:18034455 source Swiss-Prot : SWS_FT_FI1 16) chain B residue 293 type MOD_RES sequence E description Phosphotyrosine => ECO:0007744|PubMed:18034455 source Swiss-Prot : SWS_FT_FI1 17) chain B residue 364 type MOD_RES sequence G description Phosphotyrosine => ECO:0007744|PubMed:18034455 source Swiss-Prot : SWS_FT_FI1 18) chain A residue 86 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P06761 source Swiss-Prot : SWS_FT_FI3 19) chain B residue 86 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P06761 source Swiss-Prot : SWS_FT_FI3 20) chain A residue 125 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P20029 source Swiss-Prot : SWS_FT_FI4 21) chain A residue 213 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P20029 source Swiss-Prot : SWS_FT_FI4 22) chain A residue 326 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P20029 source Swiss-Prot : SWS_FT_FI4 23) chain B residue 125 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P20029 source Swiss-Prot : SWS_FT_FI4 24) chain B residue 213 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P20029 source Swiss-Prot : SWS_FT_FI4 25) chain B residue 326 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P20029 source Swiss-Prot : SWS_FT_FI4 26) chain A residue 160 type MOD_RES sequence Y description 3'-nitrotyrosine => ECO:0000250|UniProtKB:P20029 source Swiss-Prot : SWS_FT_FI5 27) chain B residue 160 type MOD_RES sequence Y description 3'-nitrotyrosine => ECO:0000250|UniProtKB:P20029 source Swiss-Prot : SWS_FT_FI5 28) chain A residue 271 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P0DMV8 source Swiss-Prot : SWS_FT_FI6 29) chain B residue 271 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P0DMV8 source Swiss-Prot : SWS_FT_FI6 30) chain A residue 353 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P20029 source Swiss-Prot : SWS_FT_FI7 31) chain B residue 353 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P20029 source Swiss-Prot : SWS_FT_FI7 32) chain A residue 352 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0000250|UniProtKB:P11021 source Swiss-Prot : SWS_FT_FI8 33) chain B residue 352 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0000250|UniProtKB:P11021 source Swiss-Prot : SWS_FT_FI8 34) chain A residue 33-40 type prosite sequence IDLGTTYS description HSP70_1 Heat shock hsp70 proteins family signature 1. IDLGTTyS source prosite : PS00297 35) chain A residue 222-235 type prosite sequence VFDLGGGTFDVSLL description HSP70_2 Heat shock hsp70 proteins family signature 2. VFDLGGGTfdvSLL source prosite : PS00329 36) chain A residue 359-373 type prosite sequence IVLVGGSTRIPKIQQ description HSP70_3 Heat shock hsp70 proteins family signature 3. IvLvGGsTRIPkIqQ source prosite : PS01036

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