eF-site ID 6nhk-AB PDB Code 6nhk Chain A, B click to enlarge Title Mortalin nucleotide binding domain in the ADP-bound state Classification CHAPERONE Compound Stress-70 protein, mitochondrial Source (GRP75_HUMAN) Sequence A:  AVVGIDLGTTNSCVAVMEGKQAKVLENAEGARTTPSVVAF TADGERLVGMPAKRQAVTNPNNTFYATKRLIGRRYDDPEV QKDIKNVPFKIVRASNGDAWVEAHGKLYSPSQIGAFVLMK MKETAENYLGHTAKNAVITVPAYFNDSQRQATKDAGQISG LNVLRVINEPTAAALAYGLDKSEDKVIAVYDLGGGTFDIS ILEIQKGVFEVKSTNGDTFLGGEDFDQALLRHIVKEFKRE TGVDLTKDNMALQRVREAAEKAKCELSSSVQTDINLPYLT MDSSGPKHLNMKLTRAQFEGIVTDLIRRTIAPCQKAMQDA EVSKSDIGEVILVGGMTRMPKVQQTVQDLFGRAPSKAVNP DEAVAIGAAIQGGVLA B:  AVVGIDLGTTNSCVAVMEQAKVLENAEGARTTPSVVAFTA DGERLVGMPAKRQAVTNPNNTFYATKRLIGRRYDDPEVQK DIKNVPFKIVRASNGDAWVEAHGKLYSPSQIGAFVLMKMK ETAENYLGHTAKNAVITVPAYFNDSQRQATKDAGQISGLN VLRVINEPTAAALAYGLDKEDKVIAVYDLGGGTFDISILE IQKGVFEVKSTNGDTFLGGEDFDQALLRHIVKEFKRETGV DLTKDNMALQRVREAAEKAKCELSSSVQTDINLPYLTMDS SGPKHLNMKLTRAQFEGIVTDLIRRTIAPCQKAMQDAEVS KSDIGEVILVGGMTRMPKVQQTVQDLFGRAPSKAVNPDEA VAIGAAIQGGVLA Description Functional site 1) chain A residue 63 type sequence T description binding site for residue ADP A 501 source : AC1 2) chain A residue 64 type sequence N description binding site for residue ADP A 501 source : AC1 3) chain A residue 247 type sequence G description binding site for residue ADP A 501 source : AC1 4) chain A residue 313 type sequence E description binding site for residue ADP A 501 source : AC1 5) chain A residue 316 type sequence K description binding site for residue ADP A 501 source : AC1 6) chain A residue 317 type sequence C description binding site for residue ADP A 501 source : AC1 7) chain A residue 320 type sequence S description binding site for residue ADP A 501 source : AC1 8) chain A residue 388 type sequence G description binding site for residue ADP A 501 source : AC1 9) chain A residue 389 type sequence M description binding site for residue ADP A 501 source : AC1 10) chain A residue 391 type sequence R description binding site for residue ADP A 501 source : AC1 11) chain A residue 414 type sequence D description binding site for residue ADP A 501 source : AC1 12) chain A residue 61 type sequence G description binding site for residue PO4 A 502 source : AC2 13) chain A residue 62 type sequence T description binding site for residue PO4 A 502 source : AC2 14) chain A residue 121 type sequence K description binding site for residue PO4 A 502 source : AC2 15) chain A residue 222 type sequence E description binding site for residue PO4 A 502 source : AC2 16) chain A residue 249 type sequence T description binding site for residue PO4 A 502 source : AC2 17) chain A residue 251 type sequence D description binding site for residue PO4 A 502 source : AC2 18) chain A residue 244 type sequence D description binding site for residue MG A 503 source : AC3 19) chain A residue 196 type sequence Y description binding site for residue GOL A 504 source : AC4 20) chain A residue 251 type sequence D description binding site for residue GOL A 504 source : AC4 21) chain A residue 267 type sequence T description binding site for residue GOL A 504 source : AC4 22) chain A residue 268 type sequence N description binding site for residue GOL A 504 source : AC4 23) chain A residue 269 type sequence G description binding site for residue GOL A 504 source : AC4 24) chain B residue 63 type sequence T description binding site for residue ADP B 600 source : AC5 25) chain B residue 64 type sequence N description binding site for residue ADP B 600 source : AC5 26) chain B residue 246 type sequence G description binding site for residue ADP B 600 source : AC5 27) chain B residue 247 type sequence G description binding site for residue ADP B 600 source : AC5 28) chain B residue 313 type sequence E description binding site for residue ADP B 600 source : AC5 29) chain B residue 316 type sequence K description binding site for residue ADP B 600 source : AC5 30) chain B residue 317 type sequence C description binding site for residue ADP B 600 source : AC5 31) chain B residue 320 type sequence S description binding site for residue ADP B 600 source : AC5 32) chain B residue 387 type sequence G description binding site for residue ADP B 600 source : AC5 33) chain B residue 388 type sequence G description binding site for residue ADP B 600 source : AC5 34) chain B residue 389 type sequence M description binding site for residue ADP B 600 source : AC5 35) chain B residue 391 type sequence R description binding site for residue ADP B 600 source : AC5 36) chain B residue 414 type sequence D description binding site for residue ADP B 600 source : AC5 37) chain B residue 61 type sequence G description binding site for residue PO4 B 601 source : AC6 38) chain B residue 62 type sequence T description binding site for residue PO4 B 601 source : AC6 39) chain B residue 121 type sequence K description binding site for residue PO4 B 601 source : AC6 40) chain B residue 222 type sequence E description binding site for residue PO4 B 601 source : AC6 41) chain B residue 249 type sequence T description binding site for residue PO4 B 601 source : AC6 42) chain B residue 251 type sequence D description binding site for residue PO4 B 601 source : AC6 43) chain B residue 244 type sequence D description binding site for residue MG B 602 source : AC7 44) chain A residue 408 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI6 45) chain B residue 408 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI6 46) chain A residue 233-245 type prosite sequence DKSEDKVIAVYDL description EF_HAND_1 EF-hand calcium-binding domain. DKSEDKVIAvyDL source prosite : PS00018 47) chain A residue 58-65 type prosite sequence IDLGTTNS description HSP70_1 Heat shock hsp70 proteins family signature 1. IDLGTTnS source prosite : PS00297 48) chain A residue 242-255 type prosite sequence VYDLGGGTFDISIL description HSP70_2 Heat shock hsp70 proteins family signature 2. VYDLGGGTfdiSIL source prosite : PS00329 49) chain A residue 383-397 type prosite sequence VILVGGMTRMPKVQQ description HSP70_3 Heat shock hsp70 proteins family signature 3. ViLvGGmTRMPkVqQ source prosite : PS01036 50) chain A residue 76 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P38647 source Swiss-Prot : SWS_FT_FI1 51) chain B residue 76 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P38647 source Swiss-Prot : SWS_FT_FI1 52) chain A residue 87 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI2 53) chain B residue 87 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI2 54) chain A residue 135 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P38647 source Swiss-Prot : SWS_FT_FI3 55) chain A residue 138 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P38647 source Swiss-Prot : SWS_FT_FI3 56) chain A residue 206 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P38647 source Swiss-Prot : SWS_FT_FI3 57) chain A residue 300 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P38647 source Swiss-Prot : SWS_FT_FI3 58) chain B residue 135 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P38647 source Swiss-Prot : SWS_FT_FI3 59) chain B residue 138 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P38647 source Swiss-Prot : SWS_FT_FI3 60) chain B residue 206 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P38647 source Swiss-Prot : SWS_FT_FI3 61) chain B residue 300 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P38647 source Swiss-Prot : SWS_FT_FI3 62) chain B residue 234 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 63) chain B residue 288 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 64) chain A residue 143 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 65) chain A residue 234 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 66) chain A residue 288 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 67) chain B residue 143 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 68) chain B residue 368 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P38647 source Swiss-Prot : SWS_FT_FI5 69) chain B residue 394 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P38647 source Swiss-Prot : SWS_FT_FI5 70) chain A residue 368 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P38647 source Swiss-Prot : SWS_FT_FI5 71) chain A residue 394 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P38647 source Swiss-Prot : SWS_FT_FI5

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