eF-site ID 6ag4-A PDB Code 6ag4 Chain A click to enlarge Title Crystal structure of Ard1 N-terminal acetyltransferase H88A/E127A mutant from Sulfolobus solfataricus Classification TRANSFERASE Compound N-alpha-acetyltransferase Source (NAT_SULSO) Sequence A:  DFTLRNARMDDIDQIIKINRLTLPENYPYYFFVEHLKEYG LAFFVAIVDNSVVGYIMPRIEWGFSNIKQLPSLVRKGAVV SIAVLEEYRRKGIATTLLEASMKSMKNDYNAEEIYLAVRV SNYPAIALYEKLNFKKVKVLKGYYADGEDAYLMARPL Description Functional site 1) chain A residue 33 type sequence L description binding site for residue ACO A 201 source : AC1 2) chain A residue 74 type sequence F description binding site for residue ACO A 201 source : AC1 3) chain A residue 91 type sequence S description binding site for residue ACO A 201 source : AC1 4) chain A residue 92 type sequence I description binding site for residue ACO A 201 source : AC1 5) chain A residue 93 type sequence A description binding site for residue ACO A 201 source : AC1 6) chain A residue 94 type sequence V description binding site for residue ACO A 201 source : AC1 7) chain A residue 99 type sequence R description binding site for residue ACO A 201 source : AC1 8) chain A residue 100 type sequence R description binding site for residue ACO A 201 source : AC1 9) chain A residue 101 type sequence K description binding site for residue ACO A 201 source : AC1 10) chain A residue 102 type sequence G description binding site for residue ACO A 201 source : AC1 11) chain A residue 103 type sequence I description binding site for residue ACO A 201 source : AC1 12) chain A residue 104 type sequence A description binding site for residue ACO A 201 source : AC1 13) chain A residue 105 type sequence T description binding site for residue ACO A 201 source : AC1 14) chain A residue 127 type sequence A description binding site for residue ACO A 201 source : AC1 15) chain A residue 132 type sequence N description binding site for residue ACO A 201 source : AC1 16) chain A residue 134 type sequence P description binding site for residue ACO A 201 source : AC1 17) chain A residue 138 type sequence L description binding site for residue ACO A 201 source : AC1 18) chain A residue 139 type sequence Y description binding site for residue ACO A 201 source : AC1 19) chain A residue 141 type sequence K description binding site for residue ACO A 201 source : AC1 20) chain A residue 61 type sequence S description binding site for residue SO4 A 202 source : AC2 21) chain A residue 63 type sequence V description binding site for residue SO4 A 202 source : AC2 22) chain A residue 72 type sequence W description binding site for residue SO4 A 202 source : AC2 23) chain A residue 83 type sequence L description binding site for residue SO4 A 202 source : AC2 24) chain A residue 95 type sequence L description binding site for residue SO4 A 202 source : AC2 25) chain A residue 98 type sequence Y description binding site for residue SO4 A 202 source : AC2 26) chain A residue 133 type sequence Y description binding site for residue SO4 A 202 source : AC2 27) chain A residue 129 type sequence R description binding site for residue CA A 203 source : AC3 28) chain A residue 132 type sequence N description binding site for residue CA A 203 source : AC3 29) chain A residue 37 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:25728374, ECO:0007744|PDB:4R3L source Swiss-Prot : SWS_FT_FI1 30) chain A residue 154 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:25728374, ECO:0007744|PDB:4R3L source Swiss-Prot : SWS_FT_FI1 31) chain A residue 88 type BINDING sequence A description BINDING => ECO:0000269|PubMed:23959863, ECO:0007744|PDB:4LX9 source Swiss-Prot : SWS_FT_FI2 32) chain A residue 127 type BINDING sequence A description BINDING => ECO:0000269|PubMed:23959863, ECO:0007744|PDB:4LX9 source Swiss-Prot : SWS_FT_FI2 33) chain A residue 92 type BINDING sequence I description BINDING => ECO:0000269|PubMed:20419351, ECO:0000269|PubMed:23959863, ECO:0000269|PubMed:25728374, ECO:0000269|PubMed:26593285, ECO:0007744|PDB:2X7B, ECO:0007744|PDB:4LX9, ECO:0007744|PDB:4R3K, ECO:0007744|PDB:4R3L, ECO:0007744|PDB:5C88 source Swiss-Prot : SWS_FT_FI3 34) chain A residue 100 type BINDING sequence R description BINDING => ECO:0000269|PubMed:20419351, ECO:0000269|PubMed:23959863, ECO:0000269|PubMed:25728374, ECO:0000269|PubMed:26593285, ECO:0007744|PDB:2X7B, ECO:0007744|PDB:4LX9, ECO:0007744|PDB:4R3K, ECO:0007744|PDB:4R3L, ECO:0007744|PDB:5C88 source Swiss-Prot : SWS_FT_FI3 35) chain A residue 132 type BINDING sequence N description BINDING => ECO:0000269|PubMed:20419351, ECO:0000269|PubMed:23959863, ECO:0000269|PubMed:25728374, ECO:0007744|PDB:2X7B, ECO:0007744|PDB:4LX9, ECO:0007744|PDB:4R3K, ECO:0007744|PDB:4R3L source Swiss-Prot : SWS_FT_FI4 36) chain A residue 139 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:20419351, ECO:0000269|PubMed:23959863, ECO:0000269|PubMed:25728374, ECO:0007744|PDB:2X7B, ECO:0007744|PDB:4LX9, ECO:0007744|PDB:4R3K, ECO:0007744|PDB:4R3L source Swiss-Prot : SWS_FT_FI4 37) chain A residue 35 type SITE sequence E description Plays an important role in substrate specificity => ECO:0000269|PubMed:25728374 source Swiss-Prot : SWS_FT_FI5 38) chain A residue 75 type SITE sequence S description Plays an important role in modulating multiple conformations of loop regions and contributes to protein thermostability => ECO:0000269|PubMed:26593285 source Swiss-Prot : SWS_FT_FI6 39) chain A residue 82 type SITE sequence S description Plays an important role in modulating multiple conformations of loop regions and contributes to protein thermostability => ECO:0000269|PubMed:26593285 source Swiss-Prot : SWS_FT_FI6

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