eF-site ID 4b0s-A PDB Code 4b0s Chain A click to enlarge Title Structure of the Deamidase-Depupylase Dop of the Prokaryotic Ubiquitin-like Modification Pathway in Complex with ATP Classification HYDROLASE Compound DEAMIDASE-DEPUPYLASE DOP Source (A0LU48_ACIC1) Sequence A:  MHRVMGIETEYGISVPHQPNANAMAASSQVVNAYAPANVI LTNGARLYVDHAHPEYSTPEVTNPRDAVLWDKAGERIMAE AARRAADLPMGWTIQLYKNNTDNKGASYGCHENYLMNRST PFADIVRHLIPFFVTRQVFCGAGRVGIGADGRGEGFQLSQ RADFFEVEVGLETTLKRPIINTRDEPHADPEKYRRLHVII GDANMSEIATYLKLGTTALVLAMIEDGFLSQDFSVESPVG ALRAVSHDPTLRYQLRLHDGRRLTAVQLQMEYLEQARKYV EDRFGTDVDDMTRDVLDRWETTLVRLADDPMQLSRDLDWV AKLSILEGYRQRENLPWSAHKLQLVDLQYHDVRPDRGLYN RLVARGRMNLLVDEAAVRTAMHEPPNDTRAYFRGRCLAKF GAEIAAASWDSVIFDLPGRDSLQRVPTLEPLRGTRAHVGD LLDRCRSATELVAALT Description Functional site 1) chain A residue 4 type sequence V description binding site for residue ATP A 1501 source : AC1 2) chain A residue 6 type sequence G description binding site for residue ATP A 1501 source : AC1 3) chain A residue 7 type sequence I description binding site for residue ATP A 1501 source : AC1 4) chain A residue 8 type sequence E description binding site for residue ATP A 1501 source : AC1 5) chain A residue 90 type sequence R description binding site for residue ATP A 1501 source : AC1 6) chain A residue 92 type sequence Y description binding site for residue ATP A 1501 source : AC1 7) chain A residue 94 type sequence D description binding site for residue ATP A 1501 source : AC1 8) chain A residue 99 type sequence E description binding site for residue ATP A 1501 source : AC1 9) chain A residue 101 type sequence S description binding site for residue ATP A 1501 source : AC1 10) chain A residue 102 type sequence T description binding site for residue ATP A 1501 source : AC1 11) chain A residue 103 type sequence P description binding site for residue ATP A 1501 source : AC1 12) chain A residue 157 type sequence N description binding site for residue ATP A 1501 source : AC1 13) chain A residue 159 type sequence L description binding site for residue ATP A 1501 source : AC1 14) chain A residue 227 type sequence R description binding site for residue ATP A 1501 source : AC1 15) chain A residue 230 type sequence P description binding site for residue ATP A 1501 source : AC1 16) chain A residue 239 type sequence R description binding site for residue ATP A 1501 source : AC1 17) chain A residue 433 type sequence R description binding site for residue ATP A 1501 source : AC1 18) chain A residue 453 type sequence W description binding site for residue ATP A 1501 source : AC1 19) chain A residue 8 type sequence E description binding site for residue MG A 1502 source : AC2 20) chain A residue 155 type sequence H description binding site for residue MG A 1502 source : AC2 21) chain A residue 241 type sequence H description binding site for residue MG A 1502 source : AC2 22) chain A residue 8 type sequence E description binding site for residue MG A 1503 source : AC3 23) chain A residue 92 type sequence Y description binding site for residue MG A 1503 source : AC3 24) chain A residue 99 type sequence E description binding site for residue MG A 1503 source : AC3 25) chain A residue 94 type ACT_SITE sequence D description Proton acceptor => ECO:0000305|PubMed:22910360 source Swiss-Prot : SWS_FT_FI1 26) chain A residue 8 type BINDING sequence E description BINDING => ECO:0000269|PubMed:22910360 source Swiss-Prot : SWS_FT_FI2 27) chain A residue 92 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:22910360 source Swiss-Prot : SWS_FT_FI2 28) chain A residue 99 type BINDING sequence E description BINDING => ECO:0000269|PubMed:22910360 source Swiss-Prot : SWS_FT_FI2 29) chain A residue 101 type BINDING sequence S description BINDING => ECO:0000269|PubMed:22910360 source Swiss-Prot : SWS_FT_FI2 30) chain A residue 155 type BINDING sequence H description BINDING => ECO:0000269|PubMed:22910360 source Swiss-Prot : SWS_FT_FI2 31) chain A residue 157 type BINDING sequence N description BINDING => ECO:0000269|PubMed:22910360 source Swiss-Prot : SWS_FT_FI2 32) chain A residue 239 type BINDING sequence R description BINDING => ECO:0000269|PubMed:22910360 source Swiss-Prot : SWS_FT_FI2 33) chain A residue 241 type BINDING sequence H description BINDING => ECO:0000269|PubMed:22910360 source Swiss-Prot : SWS_FT_FI2

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