eF-site ID 6gll-A PDB Code 6gll Chain A click to enlarge Title Crystal structure of hMTH1 N33A in complex with LW14 in the presence of acetate Classification HYDROLASE Compound 7,8-dihydro-8-oxoguanine triphosphatase Source (8ODP_HUMAN) Sequence A:  GAMGASRLYTLVLVLQPQRVLLGMKKRGFGAGRWAGFGGK VQEGETIEDGARRELQEESGLTVDALHKVGQIVFEFVGEP ELMDVHVFCTDSIQGTPVESDEMRPCWFQLDQIPFKDMWP DDSYWFPLLLQKKKFHGYFKFQGQDTILDYTLREVDTV Description (1)  7,8-dihydro-8-oxoguanine triphosphatase (E.C.3.6.1.55,3.6.1.56) Functional site 1) chain A residue 72 type sequence F description binding site for residue BU8 A 201 source : AC1 2) chain A residue 74 type sequence F description binding site for residue BU8 A 201 source : AC1 3) chain A residue 117 type sequence W description binding site for residue BU8 A 201 source : AC1 4) chain A residue 119 type sequence D description binding site for residue BU8 A 201 source : AC1 5) chain A residue 120 type sequence D description binding site for residue BU8 A 201 source : AC1 6) chain A residue 134 type sequence H description binding site for residue SO4 A 202 source : AC2 7) chain A residue 151 type sequence R description binding site for residue SO4 A 202 source : AC2 8) chain A residue 9 type sequence L description binding site for residue ACT A 203 source : AC3 9) chain A residue 33 type sequence A description binding site for residue ACT A 203 source : AC3 10) chain A residue 34 type sequence G description binding site for residue ACT A 203 source : AC3 11) chain A residue 120 type sequence D description binding site for residue ACT A 203 source : AC3 12) chain A residue 123 type sequence W description binding site for residue ACT A 203 source : AC3 13) chain A residue 44 type sequence T description binding site for residue SO4 B 202 source : AC5 14) chain A residue 45 type sequence I description binding site for residue SO4 B 202 source : AC5 15) chain A residue 130 type sequence K description binding site for residue SO4 B 203 source : AC6 16) chain A residue 37-58 type prosite sequence GKVQEGETIEDGARRELQEESG description NUDIX_BOX Nudix box signature. GkvqegEtiedGArRELqEEsG source prosite : PS00893 17) chain A residue 102 type BINDING sequence R description BINDING => ECO:0000269|PubMed:30304478, ECO:0007744|PDB:5OTM source Swiss-Prot : SWS_FT_FI1 18) chain A residue 8 type BINDING sequence T description BINDING => ECO:0000269|PubMed:30304478, ECO:0007744|PDB:5OTM source Swiss-Prot : SWS_FT_FI1 19) chain A residue 18 type BINDING sequence V description BINDING => ECO:0000269|PubMed:30304478, ECO:0007744|PDB:5OTM source Swiss-Prot : SWS_FT_FI1 20) chain A residue 12 type BINDING sequence V description BINDING => ECO:0000269|PubMed:26999531, ECO:0007744|PDB:5FSK source Swiss-Prot : SWS_FT_FI2 21) chain A residue 20 type BINDING sequence L description BINDING => ECO:0000269|PubMed:26999531, ECO:0000269|PubMed:28035004, ECO:0007744|PDB:5FSI, ECO:0007744|PDB:5GHI, ECO:0007744|PDB:5GHM source Swiss-Prot : SWS_FT_FI3 22) chain A residue 85 type BINDING sequence V description BINDING => ECO:0000250|UniProtKB:Q7ZWC3 source Swiss-Prot : SWS_FT_FI4 23) chain A residue 37 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:Q7ZWC3 source Swiss-Prot : SWS_FT_FI4 24) chain A residue 40 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:Q7ZWC3 source Swiss-Prot : SWS_FT_FI4 25) chain A residue 41 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:Q7ZWC3 source Swiss-Prot : SWS_FT_FI4 26) chain A residue 21 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:Q7ZWC3 source Swiss-Prot : SWS_FT_FI4

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