eF-site ID 5bom-ADPT PDB Code 5bom Chain A, D, P, T click to enlarge Title DNA polymerase beta binary complex with a templating 5ClC Classification TRANSFERASE, LYASE/DNA Compound DNA polymerase beta Source (5BOM) Sequence A:  LNGGITDMLTELANFEKNVSQAIHKYNAYRKAASVIAKYP HKIKSGAEAKKLPGVGTKIAEKIDEFLATGKLRKLEKIRQ DDTSSSINFLTRVSGIGPSAARKFVDEGIKTLEDLRKNED KLNHHQRIGLKYFGDFEKRIPREEMLQMQDIVLNEVKKVD SEYIATVCGSFRRGAESSGDMDVLLTHPSFTSESPKLLHQ VVEQLQKVHFITDTLSKGETKFMGVCQLPSDEKEYPHRRI DIRLIPKDQYYCGVLYFTGSDIFNKNMRAHALEKGFTINE YTIRPLGVTGVAGEPLPVDSEKDIFDYIQWKYREPKDRSE D:  GTCGG P:  GCTGATGCGC T:  CCGACXGCGCATCAGC Description Functional site 1) chain A residue 101 type sequence T description binding site for residue NA A 401 source : AC1 2) chain A residue 103 type sequence V description binding site for residue NA A 401 source : AC1 3) chain A residue 106 type sequence I description binding site for residue NA A 401 source : AC1 4) chain P residue 9 type sequence G description binding site for residue NA A 401 source : AC1 5) chain A residue 60 type sequence K description binding site for residue NA A 402 source : AC2 6) chain A residue 62 type sequence L description binding site for residue NA A 402 source : AC2 7) chain A residue 65 type sequence V description binding site for residue NA A 402 source : AC2 8) chain D residue 3 type sequence C description binding site for residue NA A 402 source : AC2 9) chain A residue 179-198 type prosite sequence GSFRRGAESSGDMDVLLTHP description DNA_POLYMERASE_X DNA polymerase family X signature. GSFrRGaesSgDMDVLLthP source prosite : PS00522 10) chain A residue 72 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:Q8K409 source Swiss-Prot : SWS_FT_FI6 11) 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 12) 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 13) 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 14) 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 15) 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 16) chain A residue 183 type BINDING sequence R description BINDING => ECO:0000269|PubMed:8841119, ECO:0007744|PDB:8ICX source Swiss-Prot : SWS_FT_FI4 17) chain A residue 190 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9287163, ECO:0007744|PDB:1BPY source Swiss-Prot : SWS_FT_FI5 18) chain A residue 192 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9287163, ECO:0007744|PDB:1BPY source Swiss-Prot : SWS_FT_FI5 19) chain A residue 256 type BINDING sequence D description BINDING => ECO:0000269|PubMed:9287163, ECO:0007744|PDB:1BPY source Swiss-Prot : SWS_FT_FI5 20) 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 21) 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 22) 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 23) 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 24) 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 25) 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 26) 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 27) 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 28) 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 29) 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

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