eF-site ID 6do2-B PDB Code 6do2 Chain B click to enlarge Title Crystal structure of human GRP78 in complex with 7-deaza-2'-C-methyladenosine Classification chaperone, hydrolase Compound Endoplasmic reticulum chaperone BiP Source (BIP_HUMAN) Sequence B:  DVGTVVGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSY VAFTPEGERLIGDAAKNQLTSNPENTVFDAKRLIGRTWND PSVQQDIKFLPFKVVEKKTKPYIQVDIGGGQTKTFAPEEI SAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATK DAGTIAGLNVMRIINEPTAAAIAYGLDKREGEKNILVFDL GGGTFDVSLLTIDNGVFEVVATNGDTHLGGEDFDQRVMEH FIKLYKKKTGKDVRKDNRAVQKLRREVEKAKRALSSQHQA RIEIESFYEGEDFSETLTRAKFEELNMDLFRSTMKPVQKV LEDSDLKKSDIDEIVLVGGSTRIPKIQQLVKEFFNGKEPS RGINPDEAVAYGAAVQAGVLSG Description Functional site 1) chain B residue 39 type sequence Y description binding site for residue H5V B 501 source : AC2 2) chain B residue 255 type sequence G description binding site for residue H5V B 501 source : AC2 3) chain B residue 293 type sequence E description binding site for residue H5V B 501 source : AC2 4) chain B residue 296 type sequence K description binding site for residue H5V B 501 source : AC2 5) chain B residue 297 type sequence R description binding site for residue H5V B 501 source : AC2 6) chain B residue 300 type sequence S description binding site for residue H5V B 501 source : AC2 7) chain B residue 364 type sequence G description binding site for residue H5V B 501 source : AC2 8) chain B residue 365 type sequence S description binding site for residue H5V B 501 source : AC2 9) chain B residue 367 type sequence R description binding site for residue H5V B 501 source : AC2 10) chain B residue 391 type sequence D description binding site for residue H5V B 501 source : AC2 11) chain B residue 271 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P0DMV8 source Swiss-Prot : SWS_FT_FI5 12) chain B residue 353 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P20029 source Swiss-Prot : SWS_FT_FI6 13) 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 14) 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 15) chain B residue 364 type BINDING sequence G description BINDING => ECO:0000269|PubMed:21526763 source Swiss-Prot : SWS_FT_FI1 16) chain B residue 293 type BINDING sequence E description BINDING => ECO:0000269|PubMed:21526763 source Swiss-Prot : SWS_FT_FI1 17) chain B residue 227 type BINDING sequence G description BINDING => ECO:0000269|PubMed:21526763 source Swiss-Prot : SWS_FT_FI1 18) chain B residue 36 type BINDING sequence G description BINDING => ECO:0000269|PubMed:21526763 source Swiss-Prot : SWS_FT_FI1 19) chain B residue 96 type BINDING sequence K description BINDING => ECO:0000269|PubMed:21526763 source Swiss-Prot : SWS_FT_FI1 20) chain B residue 86 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P06761 source Swiss-Prot : SWS_FT_FI2 21) chain B residue 125 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P20029 source Swiss-Prot : SWS_FT_FI3 22) chain B residue 213 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P20029 source Swiss-Prot : SWS_FT_FI3 23) chain B residue 326 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P20029 source Swiss-Prot : SWS_FT_FI3 24) chain B residue 160 type MOD_RES sequence Y description 3'-nitrotyrosine => ECO:0000250|UniProtKB:P20029 source Swiss-Prot : SWS_FT_FI4

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