eF-site ID 6cub-ADPT PDB Code 6cub Chain A, D, P, T click to enlarge Title Structure of human DNA polymerase beta complexed with 8-ClG in the template base paired with incoming non-hydrolyzable ATP and MANGANESE Classification Transferase, Lyase/DNA Compound DNA polymerase beta Source (6CUB) Sequence A:  PQETLNGGITDMLTELANFEKNVSQAIHKYNAYRKAASVI AKYPHKIKSGAEAKKLPGVGTKIAEKIDEFLATGKLRKLE KIRQDDTSSSINFLTRVSGIGPSAARKFVDEGIKTLEDLR KNEDKLNHHQRIGLKYFGDFEKRIPREEMLQMQDIVLNEV KKVDSEYIATVCGSFRRGAESSGDMDVLLTHPSFTSESQP KLLHQVVEQLQKVHFITDTLSKGETKFMGVCQLPSKNDEK EYPHRRIDIRLIPKDQYYCGVLYFTGSDIFNKNMRAHALE KGFTINEYTIRPLGVTGVAGEPLPVDSEKDIFDYIQWKYR EPKDRSE D:  GTCGG P:  GCTGATGCGA T:  CCGACXTCGCATCAGC Description Functional site 1) chain A residue 179 type sequence G description binding site for residue DZ4 A 401 source : AC1 2) chain A residue 180 type sequence S description binding site for residue DZ4 A 401 source : AC1 3) chain A residue 183 type sequence R description binding site for residue DZ4 A 401 source : AC1 4) chain A residue 188 type sequence S description binding site for residue DZ4 A 401 source : AC1 5) chain A residue 189 type sequence G description binding site for residue DZ4 A 401 source : AC1 6) chain A residue 190 type sequence D description binding site for residue DZ4 A 401 source : AC1 7) chain A residue 192 type sequence D description binding site for residue DZ4 A 401 source : AC1 8) chain A residue 271 type sequence Y description binding site for residue DZ4 A 401 source : AC1 9) chain A residue 272 type sequence F description binding site for residue DZ4 A 401 source : AC1 10) chain A residue 274 type sequence G description binding site for residue DZ4 A 401 source : AC1 11) chain A residue 276 type sequence D description binding site for residue DZ4 A 401 source : AC1 12) chain A residue 279 type sequence N description binding site for residue DZ4 A 401 source : AC1 13) chain A residue 280 type sequence K description binding site for residue DZ4 A 401 source : AC1 14) chain P residue 10 type sequence A description binding site for residue DZ4 A 401 source : AC1 15) chain A residue 190 type sequence D description binding site for residue MN A 402 source : AC2 16) chain A residue 192 type sequence D description binding site for residue MN A 402 source : AC2 17) chain A residue 190 type sequence D description binding site for residue MN A 403 source : AC3 18) chain A residue 192 type sequence D description binding site for residue MN A 403 source : AC3 19) chain P residue 10 type sequence A description binding site for residue MN A 403 source : AC3 20) chain A residue 101 type sequence T description binding site for residue NA A 404 source : AC4 21) chain A residue 103 type sequence V description binding site for residue NA A 404 source : AC4 22) chain A residue 106 type sequence I description binding site for residue NA A 404 source : AC4 23) chain P residue 9 type sequence G description binding site for residue NA A 404 source : AC4 24) chain A residue 60 type sequence K description binding site for residue NA A 405 source : AC5 25) chain A residue 62 type sequence L description binding site for residue NA A 405 source : AC5 26) chain A residue 65 type sequence V description binding site for residue NA A 405 source : AC5 27) chain D residue 3 type sequence C description binding site for residue NA A 405 source : AC5 28) chain A residue 72 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:Q8K409 source Swiss-Prot : SWS_FT_FI6 29) chain A residue 83 type MOD_RES sequence R description Omega-N-methylarginine; by PRMT6 => ECO:0000269|PubMed:16600869 source Swiss-Prot : SWS_FT_FI7 30) chain A residue 152 type MOD_RES sequence R description Omega-N-methylarginine; by PRMT6 => ECO:0000269|PubMed:16600869 source Swiss-Prot : SWS_FT_FI7 31) chain A residue 41 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:19713937, ECO:0000269|PubMed:21362556 source Swiss-Prot : SWS_FT_FI8 32) chain A residue 61 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:19713937, ECO:0000269|PubMed:21362556 source Swiss-Prot : SWS_FT_FI8 33) chain A residue 81 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:19713937, ECO:0000269|PubMed:21362556 source Swiss-Prot : SWS_FT_FI8 34) chain A residue 179-198 type prosite sequence GSFRRGAESSGDMDVLLTHP description DNA_POLYMERASE_X DNA polymerase family X signature. GSFrRGaesSgDMDVLLthP source prosite : PS00522 35) chain A residue 72 type ACT_SITE sequence K description Nucleophile; Schiff-base intermediate with DNA; for 5'-dRP lyase activity => ECO:0000269|PubMed:9572863 source Swiss-Prot : SWS_FT_FI1 36) chain A residue 101 type BINDING sequence T description BINDING => ECO:0000269|PubMed:12517346, ECO:0000269|PubMed:8841120, ECO:0000269|PubMed:9287163, ECO:0007744|PDB:1BPX, ECO:0007744|PDB:1BPZ, ECO:0007744|PDB:1MQ3, ECO:0007744|PDB:1ZQO, ECO:0007744|PDB:1ZQQ source Swiss-Prot : SWS_FT_FI2 37) chain A residue 103 type BINDING sequence V description BINDING => ECO:0000269|PubMed:12517346, ECO:0000269|PubMed:8841120, ECO:0000269|PubMed:9287163, ECO:0007744|PDB:1BPX, ECO:0007744|PDB:1BPZ, ECO:0007744|PDB:1MQ3, ECO:0007744|PDB:1ZQO, ECO:0007744|PDB:1ZQQ source Swiss-Prot : SWS_FT_FI2 38) chain A residue 106 type BINDING sequence I description BINDING => ECO:0000269|PubMed:12517346, ECO:0000269|PubMed:8841120, ECO:0000269|PubMed:9287163, ECO:0007744|PDB:1BPX, ECO:0007744|PDB:1BPZ, ECO:0007744|PDB:1MQ3, ECO:0007744|PDB:1ZQO, ECO:0007744|PDB:1ZQQ source Swiss-Prot : SWS_FT_FI2 39) chain A residue 60 type BINDING sequence K description BINDING => ECO:0000269|PubMed:12517346, ECO:0000269|PubMed:8841120, ECO:0000269|PubMed:9287163, ECO:0007744|PDB:1BPX, ECO:0007744|PDB:1BPZ, ECO:0007744|PDB:1MQ3, ECO:0007744|PDB:1ZQO, ECO:0007744|PDB:1ZQQ source Swiss-Prot : SWS_FT_FI2 40) chain A residue 62 type BINDING sequence L description BINDING => ECO:0000269|PubMed:12517346, ECO:0000269|PubMed:8841120, ECO:0000269|PubMed:9287163, ECO:0007744|PDB:1BPX, ECO:0007744|PDB:1BPZ, ECO:0007744|PDB:1MQ3, ECO:0007744|PDB:1ZQO, ECO:0007744|PDB:1ZQQ source Swiss-Prot : SWS_FT_FI2 41) chain A residue 65 type BINDING sequence V description BINDING => ECO:0000269|PubMed:12517346, ECO:0000269|PubMed:8841120, ECO:0000269|PubMed:9287163, ECO:0007744|PDB:1BPX, ECO:0007744|PDB:1BPZ, ECO:0007744|PDB:1MQ3, ECO:0007744|PDB:1ZQO, ECO:0007744|PDB:1ZQQ source Swiss-Prot : SWS_FT_FI2 42) chain A residue 180 type BINDING sequence S description BINDING => ECO:0000269|PubMed:8841119, ECO:0007744|PDB:8ICW, ECO:0007744|PDB:8ICX, ECO:0007744|PDB:8ICY source Swiss-Prot : SWS_FT_FI3 43) chain A residue 189 type BINDING sequence G description BINDING => ECO:0000269|PubMed:8841119, ECO:0007744|PDB:8ICW, ECO:0007744|PDB:8ICX, ECO:0007744|PDB:8ICY source Swiss-Prot : SWS_FT_FI3 44) chain A residue 149 type BINDING sequence R description BINDING => ECO:0000269|PubMed:8841119, ECO:0007744|PDB:8ICW, ECO:0007744|PDB:8ICX, ECO:0007744|PDB:8ICY source Swiss-Prot : SWS_FT_FI3 45) chain A residue 183 type BINDING sequence R description BINDING => ECO:0000269|PubMed:8841119, ECO:0007744|PDB:8ICX source Swiss-Prot : SWS_FT_FI4 46) chain A residue 256 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9287163, ECO:0007744|PDB:1BPY source Swiss-Prot : SWS_FT_FI5 47) chain A residue 192 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9287163, ECO:0007744|PDB:1BPY source Swiss-Prot : SWS_FT_FI5 48) chain A residue 190 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9287163, ECO:0007744|PDB:1BPY source Swiss-Prot : SWS_FT_FI5

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