eF-site ID 4ymn-A PDB Code 4ymn Chain A click to enlarge Title Structure of human DNA polymerase beta complexed with N7BG in the template base paired with incoming non-hydrolyzable CTP Classification TRANSFERASE/DNA Compound DNA polymerase beta Source (4YMN) Sequence A:  PQETLNGGITDMLTELANFEKNVSQAIHKYNAYRKAASVI AKYPHKIKSGAEAKKLPGVGTKIAEKIDEFLATGKLRKLE KIRQDDTSSSINFLTRVSGIGPSAARKFVDEGIKTLEDLR KNEDKLNHHQRIGLKYFGDFEKRIPREEMLQMQDIVLNEV KKVDSEYIATVCGSFRRGAESSGDMDVLLTHPSFTSESQP KLLHQVVEQLQKVHFITDTLSKGETKFMGVCQLPSKNDEK EYPHRRIDIRLIPKDQYYCGVLYFTGSDIFNKNMRAHALE KGFTINEYTIRPLGVTGVAGEPLPVDSEKDIFDYIQWKYR EPKDRSE Description Functional site 1) chain A residue 190 type sequence D description binding site for residue MG A 401 source : AC1 2) chain A residue 101 type sequence T description binding site for residue NA A 402 source : AC2 3) chain A residue 103 type sequence V description binding site for residue NA A 402 source : AC2 4) chain A residue 106 type sequence I description binding site for residue NA A 402 source : AC2 5) chain A residue 60 type sequence K description binding site for residue NA A 403 source : AC3 6) chain A residue 61 type sequence K description binding site for residue NA A 403 source : AC3 7) chain A residue 62 type sequence L description binding site for residue NA A 403 source : AC3 8) chain A residue 65 type sequence V description binding site for residue NA A 403 source : AC3 9) chain A residue 149 type sequence R description binding site for residue 0KX A 404 source : AC4 10) chain A residue 180 type sequence S description binding site for residue 0KX A 404 source : AC4 11) chain A residue 183 type sequence R description binding site for residue 0KX A 404 source : AC4 12) chain A residue 188 type sequence S description binding site for residue 0KX A 404 source : AC4 13) chain A residue 189 type sequence G description binding site for residue 0KX A 404 source : AC4 14) chain A residue 190 type sequence D description binding site for residue 0KX A 404 source : AC4 15) chain A residue 271 type sequence Y description binding site for residue 0KX A 404 source : AC4 16) chain A residue 274 type sequence G description binding site for residue 0KX A 404 source : AC4 17) chain A residue 276 type sequence D description binding site for residue 0KX A 404 source : AC4 18) chain A residue 72 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:Q8K409 source Swiss-Prot : SWS_FT_FI6 19) 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 20) 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 21) 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 22) 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 23) 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 24) chain A residue 183 type BINDING sequence R description BINDING => ECO:0000269|PubMed:8841119, ECO:0007744|PDB:8ICX source Swiss-Prot : SWS_FT_FI4 25) chain A residue 192 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9287163, ECO:0007744|PDB:1BPY source Swiss-Prot : SWS_FT_FI5 26) chain A residue 190 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9287163, ECO:0007744|PDB:1BPY source Swiss-Prot : SWS_FT_FI5 27) chain A residue 256 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9287163, ECO:0007744|PDB:1BPY source Swiss-Prot : SWS_FT_FI5 28) chain A residue 179-198 type prosite sequence GSFRRGAESSGDMDVLLTHP description DNA_POLYMERASE_X DNA polymerase family X signature. GSFrRGaesSgDMDVLLthP source prosite : PS00522 29) 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 30) 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 31) 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 32) 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 33) 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 34) 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 35) 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 36) 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 37) 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 38) 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

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