eF-site ID 2ak3-B PDB Code 2ak3 Chain B click to enlarge Title THE THREE-DIMENSIONAL STRUCTURE OF THE COMPLEX BETWEEN MITOCHONDRIAL MATRIX ADENYLATE KINASE AND ITS SUBSTRATE AMP AT 1.85 ANGSTROMS RESOLUTION Classification TRANSFERASE (PHOSPHOTRANSFERASE) Compound ADENYLATE KINASE ISOENZYME-3 Source null (KAD3_BOVIN) Sequence B:  GASARLLRAAIMGAPGSGKGTVSSRITKHFELKHLSSGDL LRDNMLRGTEIGVLAKTFIDQGKLIPDDVMTRLVLHELKN LTQYNWLLDGFPRTLPQAEALDRAYQIDTVINLNVPFEVI KQRLTARWIHPGSGRVYNIEFNPPKTMGIDDLTGEPLVQR EDDRPETVVKRLKAYEAQTEPVLEYYRKKGVLETFSGTET NKIWPHVYAFLQTKLPQRSQE Description Functional site 1) chain B residue 15 type sequence G description BINDING SITE FOR RESIDUE SO4 B 227 source : AC2 2) chain B residue 16 type sequence S description BINDING SITE FOR RESIDUE SO4 B 227 source : AC2 3) chain B residue 17 type sequence G description BINDING SITE FOR RESIDUE SO4 B 227 source : AC2 4) chain B residue 18 type sequence K description BINDING SITE FOR RESIDUE SO4 B 227 source : AC2 5) chain B residue 19 type sequence G description BINDING SITE FOR RESIDUE SO4 B 227 source : AC2 6) chain B residue 36 type sequence S description BINDING SITE FOR RESIDUE AMP B 226 source : AC4 7) chain B residue 37 type sequence G description BINDING SITE FOR RESIDUE AMP B 226 source : AC4 8) chain B residue 40 type sequence L description BINDING SITE FOR RESIDUE AMP B 226 source : AC4 9) chain B residue 41 type sequence R description BINDING SITE FOR RESIDUE AMP B 226 source : AC4 10) chain B residue 58 type sequence I description BINDING SITE FOR RESIDUE AMP B 226 source : AC4 11) chain B residue 62 type sequence K description BINDING SITE FOR RESIDUE AMP B 226 source : AC4 12) chain B residue 63 type sequence L description BINDING SITE FOR RESIDUE AMP B 226 source : AC4 13) chain B residue 64 type sequence I description BINDING SITE FOR RESIDUE AMP B 226 source : AC4 14) chain B residue 69 type sequence M description BINDING SITE FOR RESIDUE AMP B 226 source : AC4 15) chain B residue 89 type sequence G description BINDING SITE FOR RESIDUE AMP B 226 source : AC4 16) chain B residue 92 type sequence R description BINDING SITE FOR RESIDUE AMP B 226 source : AC4 17) chain B residue 96 type sequence Q description BINDING SITE FOR RESIDUE AMP B 226 source : AC4 18) chain B residue 42 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_03169 source Swiss-Prot : SWS_FT_FI1 19) chain B residue 90 type BINDING sequence F description BINDING => ECO:0000255|HAMAP-Rule:MF_03169 source Swiss-Prot : SWS_FT_FI1 20) chain B residue 127 type BINDING sequence W description BINDING => ECO:0000255|HAMAP-Rule:MF_03169 source Swiss-Prot : SWS_FT_FI1 21) chain B residue 136 type BINDING sequence Y description BINDING => ECO:0000255|HAMAP-Rule:MF_03169 source Swiss-Prot : SWS_FT_FI1 22) chain B residue 160 type BINDING sequence E description BINDING => ECO:0000255|HAMAP-Rule:MF_03169 source Swiss-Prot : SWS_FT_FI1 23) chain B residue 171 type BINDING sequence L description BINDING => ECO:0000255|HAMAP-Rule:MF_03169 source Swiss-Prot : SWS_FT_FI1 24) chain B residue 200 type BINDING sequence N description BINDING => ECO:0000255|HAMAP-Rule:MF_03169 source Swiss-Prot : SWS_FT_FI1 25) chain B residue 16 type BINDING sequence S description BINDING => ECO:0000255|HAMAP-Rule:MF_03169 source Swiss-Prot : SWS_FT_FI1 26) chain B residue 37 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_03169, ECO:0000269|PubMed:1994037 source Swiss-Prot : SWS_FT_FI2 27) chain B residue 63 type BINDING sequence L description BINDING => ECO:0000255|HAMAP-Rule:MF_03169, ECO:0000269|PubMed:1994037 source Swiss-Prot : SWS_FT_FI2 28) chain B residue 97 type BINDING sequence A description BINDING => ECO:0000255|HAMAP-Rule:MF_03169, ECO:0000269|PubMed:1994037 source Swiss-Prot : SWS_FT_FI2 29) chain B residue 19 type MOD_RES sequence G description N6-succinyllysine => ECO:0000250|UniProtKB:Q9WTP7 source Swiss-Prot : SWS_FT_FI3 30) chain B residue 56 type MOD_RES sequence T description N6-succinyllysine => ECO:0000250|UniProtKB:Q9WTP7 source Swiss-Prot : SWS_FT_FI3 31) chain B residue 188 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9WTP7 source Swiss-Prot : SWS_FT_FI4 32) chain B residue 28 type MOD_RES sequence H description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9WTP7 source Swiss-Prot : SWS_FT_FI4 33) chain B residue 63 type MOD_RES sequence L description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9WTP7 source Swiss-Prot : SWS_FT_FI4 34) chain B residue 79 type MOD_RES sequence N description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9WTP7 source Swiss-Prot : SWS_FT_FI4 35) chain B residue 173 type MOD_RES sequence A description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9WTP7 source Swiss-Prot : SWS_FT_FI4 36) chain B residue 33 type MOD_RES sequence H description N6-acetyllysine => ECO:0000250|UniProtKB:Q9WTP7 source Swiss-Prot : SWS_FT_FI5 37) chain B residue 202 type MOD_RES sequence I description N6-acetyllysine => ECO:0000250|UniProtKB:Q9WTP7 source Swiss-Prot : SWS_FT_FI5 38) chain B residue 36 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:Q9WTP7 source Swiss-Prot : SWS_FT_FI6

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