eF-site ID 2ak3-A PDB Code 2ak3 Chain A 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 Bos taurus (Bovine) (KAD3_BOVIN) Sequence A:  GASARLLRAAIMGAPGSGKGTVSSRITKHFELKHLSSGDL LRDNMLRGTEIGVLAKTFIDQGKLIPDDVMTRLVLHELKN LTQYNWLLDGFPRTLPQAEALDRAYQIDTVINLNVPFEVI KQRLTARWIHPGSGRVYNIEFNPPKTMGIDDLTGEPLVQR EDDRPETVVKRLKAYEAQTEPVLEYYRKKGVLETFSGTET NKIWPHVYAFLQTKLPQRSQETSVTP Description Functional site 1) chain A residue 13 type sequence A description BINDING SITE FOR RESIDUE SO4 A 227 source : AC1 2) chain A residue 15 type sequence G description BINDING SITE FOR RESIDUE SO4 A 227 source : AC1 3) chain A residue 16 type sequence S description BINDING SITE FOR RESIDUE SO4 A 227 source : AC1 4) chain A residue 17 type sequence G description BINDING SITE FOR RESIDUE SO4 A 227 source : AC1 5) chain A residue 18 type sequence K description BINDING SITE FOR RESIDUE SO4 A 227 source : AC1 6) chain A residue 19 type sequence G description BINDING SITE FOR RESIDUE SO4 A 227 source : AC1 7) chain A residue 36 type sequence S description BINDING SITE FOR RESIDUE AMP A 226 source : AC3 8) chain A residue 40 type sequence L description BINDING SITE FOR RESIDUE AMP A 226 source : AC3 9) chain A residue 41 type sequence R description BINDING SITE FOR RESIDUE AMP A 226 source : AC3 10) chain A residue 58 type sequence I description BINDING SITE FOR RESIDUE AMP A 226 source : AC3 11) chain A residue 62 type sequence K description BINDING SITE FOR RESIDUE AMP A 226 source : AC3 12) chain A residue 63 type sequence L description BINDING SITE FOR RESIDUE AMP A 226 source : AC3 13) chain A residue 64 type sequence I description BINDING SITE FOR RESIDUE AMP A 226 source : AC3 14) chain A residue 69 type sequence M description BINDING SITE FOR RESIDUE AMP A 226 source : AC3 15) chain A residue 89 type sequence G description BINDING SITE FOR RESIDUE AMP A 226 source : AC3 16) chain A residue 92 type sequence R description BINDING SITE FOR RESIDUE AMP A 226 source : AC3 17) chain A residue 96 type sequence Q description BINDING SITE FOR RESIDUE AMP A 226 source : AC3 18) chain A residue 37 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_03169, ECO:0000269|PubMed:1994037 source Swiss-Prot : SWS_FT_FI2 19) chain A residue 63 type BINDING sequence L description BINDING => ECO:0000255|HAMAP-Rule:MF_03169, ECO:0000269|PubMed:1994037 source Swiss-Prot : SWS_FT_FI2 20) chain A residue 97 type BINDING sequence A description BINDING => ECO:0000255|HAMAP-Rule:MF_03169, ECO:0000269|PubMed:1994037 source Swiss-Prot : SWS_FT_FI2 21) chain A residue 19 type MOD_RES sequence G description N6-succinyllysine => ECO:0000250|UniProtKB:Q9WTP7 source Swiss-Prot : SWS_FT_FI3 22) chain A residue 56 type MOD_RES sequence T description N6-succinyllysine => ECO:0000250|UniProtKB:Q9WTP7 source Swiss-Prot : SWS_FT_FI3 23) chain A residue 28 type MOD_RES sequence H description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9WTP7 source Swiss-Prot : SWS_FT_FI4 24) chain A residue 63 type MOD_RES sequence L description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9WTP7 source Swiss-Prot : SWS_FT_FI4 25) chain A residue 79 type MOD_RES sequence N description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9WTP7 source Swiss-Prot : SWS_FT_FI4 26) chain A residue 173 type MOD_RES sequence A description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9WTP7 source Swiss-Prot : SWS_FT_FI4 27) chain A residue 188 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9WTP7 source Swiss-Prot : SWS_FT_FI4 28) chain A residue 16 type BINDING sequence S description BINDING => ECO:0000255|HAMAP-Rule:MF_03169 source Swiss-Prot : SWS_FT_FI1 29) chain A residue 42 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_03169 source Swiss-Prot : SWS_FT_FI1 30) chain A residue 90 type BINDING sequence F description BINDING => ECO:0000255|HAMAP-Rule:MF_03169 source Swiss-Prot : SWS_FT_FI1 31) chain A residue 127 type BINDING sequence W description BINDING => ECO:0000255|HAMAP-Rule:MF_03169 source Swiss-Prot : SWS_FT_FI1 32) chain A residue 136 type BINDING sequence Y description BINDING => ECO:0000255|HAMAP-Rule:MF_03169 source Swiss-Prot : SWS_FT_FI1 33) chain A residue 160 type BINDING sequence E description BINDING => ECO:0000255|HAMAP-Rule:MF_03169 source Swiss-Prot : SWS_FT_FI1 34) chain A residue 171 type BINDING sequence L description BINDING => ECO:0000255|HAMAP-Rule:MF_03169 source Swiss-Prot : SWS_FT_FI1 35) chain A residue 200 type BINDING sequence N description BINDING => ECO:0000255|HAMAP-Rule:MF_03169 source Swiss-Prot : SWS_FT_FI1 36) chain A residue 33 type MOD_RES sequence H description N6-acetyllysine => ECO:0000250|UniProtKB:Q9WTP7 source Swiss-Prot : SWS_FT_FI5 37) chain A residue 202 type MOD_RES sequence I description N6-acetyllysine => ECO:0000250|UniProtKB:Q9WTP7 source Swiss-Prot : SWS_FT_FI5 38) chain A residue 36 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:Q9WTP7 source Swiss-Prot : SWS_FT_FI6 39) chain A residue 85-96 type prosite sequence WLLDGFPRTLPQ description ADENYLATE_KINASE Adenylate kinase signature. WLLDGFPRtlpQ source prosite : PS00113

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