eF-site ID 2fmq-A PDB Code 2fmq Chain A click to enlarge Title Sodium in active site of DNA Polymerase Beta Classification TRANSFERASE/DNA Compound 5'-D(*CP*CP*GP*AP*CP*AP*GP*CP*GP*CP*AP*TP*CP*AP*GP*C)-3' Source null (2FMQ) Sequence A:  TLNGGITDMLTELANFEKNVSQAIHKYNAYRKAASVIAKY PHKIKSGAEAKKLPGVGTKIAEKIDEFLATGKLRKLEKIR QDDTSSSINFLTRVSGIGPSAARKFVDEGIKTLEDLRKNE DKLNHHQRIGLKYFGDFEKRIPREEMLQMQDIVLNEVKKV DSEYIATVCGSFRRGAESSGDMDVLLTHPSFTSESTKQPK LLHQVVEQLQKVHFITDTLSKGETKFMGVCQLPSKNDEKE YPHRRIDIRLIPKDQYYCGVLYFTGSDIFNKNMRAHALEK GFTINEYTIRPLGVTGVAGEPLPVDSEKDIFDYIQWKYRE PKDRSE Description Functional site 1) chain A residue 190 type sequence D description BINDING SITE FOR RESIDUE MG A 339 source : AC1 2) chain A residue 192 type sequence D description BINDING SITE FOR RESIDUE MG A 339 source : AC1 3) chain A residue 190 type sequence D description BINDING SITE FOR RESIDUE NA A 340 source : AC2 4) chain A residue 192 type sequence D description BINDING SITE FOR RESIDUE NA A 340 source : AC2 5) chain A residue 256 type sequence D description BINDING SITE FOR RESIDUE NA A 340 source : AC2 6) chain A residue 101 type sequence T description BINDING SITE FOR RESIDUE NA A 341 source : AC3 7) chain A residue 103 type sequence V description BINDING SITE FOR RESIDUE NA A 341 source : AC3 8) chain A residue 106 type sequence I description BINDING SITE FOR RESIDUE NA A 341 source : AC3 9) chain A residue 60 type sequence K description BINDING SITE FOR RESIDUE NA A 342 source : AC4 10) chain A residue 62 type sequence L description BINDING SITE FOR RESIDUE NA A 342 source : AC4 11) chain A residue 65 type sequence V description BINDING SITE FOR RESIDUE NA A 342 source : AC4 12) chain A residue 179 type sequence G description BINDING SITE FOR RESIDUE DUP A 338 source : AC5 13) chain A residue 180 type sequence S description BINDING SITE FOR RESIDUE DUP A 338 source : AC5 14) chain A residue 183 type sequence R description BINDING SITE FOR RESIDUE DUP A 338 source : AC5 15) chain A residue 188 type sequence S description BINDING SITE FOR RESIDUE DUP A 338 source : AC5 16) chain A residue 189 type sequence G description BINDING SITE FOR RESIDUE DUP A 338 source : AC5 17) chain A residue 190 type sequence D description BINDING SITE FOR RESIDUE DUP A 338 source : AC5 18) chain A residue 192 type sequence D description BINDING SITE FOR RESIDUE DUP A 338 source : AC5 19) chain A residue 271 type sequence Y description BINDING SITE FOR RESIDUE DUP A 338 source : AC5 20) chain A residue 273 type sequence T description BINDING SITE FOR RESIDUE DUP A 338 source : AC5 21) chain A residue 274 type sequence G description BINDING SITE FOR RESIDUE DUP A 338 source : AC5 22) chain A residue 276 type sequence D description BINDING SITE FOR RESIDUE DUP A 338 source : AC5 23) chain A residue 279 type sequence N description BINDING SITE FOR RESIDUE DUP A 338 source : AC5 24) chain A residue 179-198 type prosite sequence GSFRRGAESSGDMDVLLTHP description DNA_POLYMERASE_X DNA polymerase family X signature. GSFrRGaesSgDMDVLLthP source prosite : PS00522 25) chain A residue 184 type BINDING sequence G description BINDING => ECO:0000269|PubMed:8841119, ECO:0007744|PDB:8ICX source Swiss-Prot : SWS_FT_FI4 26) chain A residue 73 type MOD_RES sequence I description N6-acetyllysine => ECO:0000250|UniProtKB:Q8K409 source Swiss-Prot : SWS_FT_FI6 27) chain A residue 84 type MOD_RES sequence K description Omega-N-methylarginine; by PRMT6 => ECO:0000269|PubMed:16600869 source Swiss-Prot : SWS_FT_FI7 28) chain A residue 153 type MOD_RES sequence E description Omega-N-methylarginine; by PRMT6 => ECO:0000269|PubMed:16600869 source Swiss-Prot : SWS_FT_FI7 29) chain A residue 42 type CROSSLNK sequence A 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 30) chain A residue 62 type CROSSLNK sequence L 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 31) chain A residue 82 type CROSSLNK sequence L 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 193 type BINDING sequence V description BINDING => ECO:0000269|PubMed:9287163, ECO:0007744|PDB:1BPY source Swiss-Prot : SWS_FT_FI5 33) chain A residue 257 type BINDING sequence I description BINDING => ECO:0000269|PubMed:9287163, ECO:0007744|PDB:1BPY source Swiss-Prot : SWS_FT_FI5 34) chain A residue 191 type BINDING sequence M description BINDING => ECO:0000269|PubMed:9287163, ECO:0007744|PDB:1BPY source Swiss-Prot : SWS_FT_FI5 35) chain A residue 73 type ACT_SITE sequence I 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 61 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 37) chain A residue 63 type BINDING sequence P 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 66 type BINDING sequence G 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 102 type BINDING sequence R 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 104 type BINDING sequence S 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 107 type BINDING sequence G 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 150 type BINDING sequence I 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 181 type BINDING sequence F 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 190 type BINDING sequence D 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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