eF-site ID 6nhk-A PDB Code 6nhk Chain A 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 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 A residue 233-245 type prosite sequence DKSEDKVIAVYDL description EF_HAND_1 EF-hand calcium-binding domain. DKSEDKVIAvyDL source prosite : PS00018 25) chain A residue 58-65 type prosite sequence IDLGTTNS description HSP70_1 Heat shock hsp70 proteins family signature 1. IDLGTTnS source prosite : PS00297 26) chain A residue 242-255 type prosite sequence VYDLGGGTFDISIL description HSP70_2 Heat shock hsp70 proteins family signature 2. VYDLGGGTfdiSIL source prosite : PS00329 27) chain A residue 383-397 type prosite sequence VILVGGMTRMPKVQQ description HSP70_3 Heat shock hsp70 proteins family signature 3. ViLvGGmTRMPkVqQ source prosite : PS01036 28) chain A residue 76 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P38647 source Swiss-Prot : SWS_FT_FI1 29) chain A residue 87 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI2 30) chain A residue 135 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P38647 source Swiss-Prot : SWS_FT_FI3 31) chain A residue 138 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P38647 source Swiss-Prot : SWS_FT_FI3 32) chain A residue 206 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P38647 source Swiss-Prot : SWS_FT_FI3 33) chain A residue 300 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P38647 source Swiss-Prot : SWS_FT_FI3 34) chain A residue 143 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 35) chain A residue 234 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 36) chain A residue 288 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 37) chain A residue 368 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P38647 source Swiss-Prot : SWS_FT_FI5 38) chain A residue 394 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P38647 source Swiss-Prot : SWS_FT_FI5 39) chain A residue 408 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI6

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