eF-site ID 6dfo-AB PDB Code 6dfo Chain A, B click to enlarge Title Crystal structure of human GRP78 in complex with 8-bromoadenosine Classification CHAPERONE Compound Endoplasmic reticulum chaperone BiP Source (BIP_HUMAN) Sequence A:  DVGTVVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSY VAFTPEGERLIGDAAKNQLTPENTVFDAKRLIGRTWNDPS VQQDIKFLPFKVVEKKTKPYIQVDIGGGQTKTFAPEEISA MVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDA GTIAGLNVMRIINEPTAAAIAYGLDKREGEKNILVFDLGG GTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEHFI KLYKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQARI EIESFYEGEDFSETLTRAKFEELNMDLFRSTMKPVQKVLE DSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFNGKEPSRG INPDEAVAYGAAVQAGVLSG B:  DVGTVVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSY VAFTPEGERLIGDAAKNQLTSNPENTVFDAKRLIGRTWND PSVQQDIKFLPFKVVEKKTKPYIQVDIGGGQTKTFAPEEI SAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATK DAGTIAGLNVMRIINEPTAAAIAYGLDKREGEKNILVFDL GGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEH FIKLYKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQA RIEIESFYEGEDFSETLTRAKFEELNMDLFRSTMKPVQKV LEDSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFNGKEPS RGINPDEAVAYGAAVQAGVLSG Description Functional site 1) chain A residue 61 type sequence I description binding site for residue GBA A 501 source : AC1 2) chain A residue 255 type sequence G description binding site for residue GBA A 501 source : AC1 3) chain A residue 293 type sequence E description binding site for residue GBA A 501 source : AC1 4) chain A residue 296 type sequence K description binding site for residue GBA A 501 source : AC1 5) chain A residue 297 type sequence R description binding site for residue GBA A 501 source : AC1 6) chain A residue 300 type sequence S description binding site for residue GBA A 501 source : AC1 7) chain A residue 364 type sequence G description binding site for residue GBA A 501 source : AC1 8) chain A residue 365 type sequence S description binding site for residue GBA A 501 source : AC1 9) chain A residue 367 type sequence R description binding site for residue GBA A 501 source : AC1 10) chain A residue 368 type sequence I description binding site for residue GBA A 501 source : AC1 11) chain B residue 61 type sequence I description binding site for residue GBA B 501 source : AC2 12) chain B residue 227 type sequence G description binding site for residue GBA B 501 source : AC2 13) chain B residue 255 type sequence G description binding site for residue GBA B 501 source : AC2 14) chain B residue 293 type sequence E description binding site for residue GBA B 501 source : AC2 15) chain B residue 296 type sequence K description binding site for residue GBA B 501 source : AC2 16) chain B residue 297 type sequence R description binding site for residue GBA B 501 source : AC2 17) chain B residue 300 type sequence S description binding site for residue GBA B 501 source : AC2 18) chain B residue 364 type sequence G description binding site for residue GBA B 501 source : AC2 19) chain B residue 365 type sequence S description binding site for residue GBA B 501 source : AC2 20) chain B residue 367 type sequence R description binding site for residue GBA B 501 source : AC2 21) chain B residue 368 type sequence I description binding site for residue GBA B 501 source : AC2 22) chain A residue 160 type MOD_RES sequence Y description 3'-nitrotyrosine => ECO:0000250|UniProtKB:P20029 source Swiss-Prot : SWS_FT_FI4 23) chain B residue 160 type MOD_RES sequence Y description 3'-nitrotyrosine => ECO:0000250|UniProtKB:P20029 source Swiss-Prot : SWS_FT_FI4 24) chain A residue 271 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P0DMV8 source Swiss-Prot : SWS_FT_FI5 25) chain B residue 271 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P0DMV8 source Swiss-Prot : SWS_FT_FI5 26) chain A residue 353 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P20029 source Swiss-Prot : SWS_FT_FI6 27) chain B residue 353 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P20029 source Swiss-Prot : SWS_FT_FI6 28) chain A residue 352 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:25114211, ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI7 29) chain B residue 352 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:25114211, ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI7 30) chain A residue 353 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate => ECO:0007744|PubMed:25114211 source Swiss-Prot : SWS_FT_FI8 31) chain B residue 353 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate => ECO:0007744|PubMed:25114211 source Swiss-Prot : SWS_FT_FI8 32) chain A residue 33-40 type prosite sequence IDLGTTYS description HSP70_1 Heat shock hsp70 proteins family signature 1. IDLGTTyS source prosite : PS00297 33) chain A residue 222-235 type prosite sequence VFDLGGGTFDVSLL description HSP70_2 Heat shock hsp70 proteins family signature 2. VFDLGGGTfdvSLL source prosite : PS00329 34) chain A residue 359-373 type prosite sequence IVLVGGSTRIPKIQQ description HSP70_3 Heat shock hsp70 proteins family signature 3. IvLvGGsTRIPkIqQ source prosite : PS01036 35) chain A residue 36 type BINDING sequence G description BINDING => ECO:0000269|PubMed:21526763 source Swiss-Prot : SWS_FT_FI1 36) chain B residue 364 type BINDING sequence G description BINDING => ECO:0000269|PubMed:21526763 source Swiss-Prot : SWS_FT_FI1 37) chain A residue 96 type BINDING sequence K description BINDING => ECO:0000269|PubMed:21526763 source Swiss-Prot : SWS_FT_FI1 38) chain A residue 227 type BINDING sequence G description BINDING => ECO:0000269|PubMed:21526763 source Swiss-Prot : SWS_FT_FI1 39) chain A residue 293 type BINDING sequence E description BINDING => ECO:0000269|PubMed:21526763 source Swiss-Prot : SWS_FT_FI1 40) chain A residue 364 type BINDING sequence G description BINDING => ECO:0000269|PubMed:21526763 source Swiss-Prot : SWS_FT_FI1 41) chain B residue 36 type BINDING sequence G description BINDING => ECO:0000269|PubMed:21526763 source Swiss-Prot : SWS_FT_FI1 42) chain B residue 96 type BINDING sequence K description BINDING => ECO:0000269|PubMed:21526763 source Swiss-Prot : SWS_FT_FI1 43) chain B residue 227 type BINDING sequence G description BINDING => ECO:0000269|PubMed:21526763 source Swiss-Prot : SWS_FT_FI1 44) chain B residue 293 type BINDING sequence E description BINDING => ECO:0000269|PubMed:21526763 source Swiss-Prot : SWS_FT_FI1 45) chain B residue 86 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P06761 source Swiss-Prot : SWS_FT_FI2 46) chain A residue 125 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P20029 source Swiss-Prot : SWS_FT_FI3 47) chain A residue 213 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P20029 source Swiss-Prot : SWS_FT_FI3 48) chain A residue 326 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P20029 source Swiss-Prot : SWS_FT_FI3 49) chain B residue 125 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P20029 source Swiss-Prot : SWS_FT_FI3 50) chain B residue 213 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P20029 source Swiss-Prot : SWS_FT_FI3 51) chain B residue 326 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P20029 source Swiss-Prot : SWS_FT_FI3

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