eF-site ID 1huo-BCD PDB Code 1huo Chain B, C, D click to enlarge Title CRYSTAL STRUCTURE OF DNA POLYMERASE BETA COMPLEXED WITH DNA AND CR-TMPPCP Classification TRANSFERASE/DNA Compound 5'-D(*AP*AP*TP*AP*GP*GP*CP*GP*TP*CP*G)-3' Source Rattus norvegicus (Rat) (1HUO) Sequence B:  TLNGGITDMLVELANFEKNVSQAIHKYNAYRKAASVIAKY PHKIKSGAEAKKLPGVGTKIAEKIDEFLATGKLRKLEKIR QDDTSSSINFLTRVTGIGPSAARKLVDEGIKTLEDLRKNE DKLNHHQRIGLKYFEDFEKRIPREEMLQMQDIVLNEVKKL DPEYIATVCGSFRRGAESSGDMDVLLTHPNFTSESSKQPK LLHRVVEQLQKVRFITDTLSKGETKFMGVCQLPSENDENE YPHRRIDIRLIPKDQYYCGVLYFTGSDIFNKNMRAHALEK GFTINEYTIRPLGVTGVAGEPLPVDSEQDIFDYIQWRYRE PKDRS C:  AGGCGTCG D:  CGACGCC Description Functional site 1) chain B residue 190 type sequence D description BINDING SITE FOR RESIDUE CR B 999 source : AC2 2) chain B residue 192 type sequence D description BINDING SITE FOR RESIDUE CR B 999 source : AC2 3) chain B residue 149 type sequence R description BINDING SITE FOR RESIDUE TTE B 338 source : AC3 4) chain B residue 179 type sequence G description BINDING SITE FOR RESIDUE TTE B 338 source : AC3 5) chain B residue 180 type sequence S description BINDING SITE FOR RESIDUE TTE B 338 source : AC3 6) chain B residue 183 type sequence R description BINDING SITE FOR RESIDUE TTE B 338 source : AC3 7) chain B residue 188 type sequence S description BINDING SITE FOR RESIDUE TTE B 338 source : AC3 8) chain B residue 189 type sequence G description BINDING SITE FOR RESIDUE TTE B 338 source : AC3 9) chain B residue 190 type sequence D description BINDING SITE FOR RESIDUE TTE B 338 source : AC3 10) chain B residue 192 type sequence D description BINDING SITE FOR RESIDUE TTE B 338 source : AC3 11) chain B residue 271 type sequence Y description BINDING SITE FOR RESIDUE TTE B 338 source : AC3 12) chain B residue 272 type sequence F description BINDING SITE FOR RESIDUE TTE B 338 source : AC3 13) chain B residue 273 type sequence T description BINDING SITE FOR RESIDUE TTE B 338 source : AC3 14) chain B residue 275 type sequence S description BINDING SITE FOR RESIDUE TTE B 338 source : AC3 15) chain B residue 276 type sequence D description BINDING SITE FOR RESIDUE TTE B 338 source : AC3 16) chain B residue 279 type sequence N description BINDING SITE FOR RESIDUE TTE B 338 source : AC3 17) chain C residue 4 type sequence A description BINDING SITE FOR RESIDUE TTE B 338 source : AC3 18) chain C residue 5 type sequence G description BINDING SITE FOR RESIDUE TTE B 338 source : AC3 19) chain D residue 7 type sequence C description BINDING SITE FOR RESIDUE TTE B 338 source : AC3 20) chain B residue 72 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:Q8K409 source Swiss-Prot : SWS_FT_FI3 21) chain B residue 83 type MOD_RES sequence R description Omega-N-methylarginine; by PRMT6 => ECO:0000250|UniProtKB:P06746 source Swiss-Prot : SWS_FT_FI4 22) chain B residue 152 type MOD_RES sequence R description Omega-N-methylarginine; by PRMT6 => ECO:0000250|UniProtKB:P06746 source Swiss-Prot : SWS_FT_FI4 23) chain B residue 41 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P06746 source Swiss-Prot : SWS_FT_FI5 24) chain B residue 61 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P06746 source Swiss-Prot : SWS_FT_FI5 25) chain B residue 81 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P06746 source Swiss-Prot : SWS_FT_FI5 26) chain B residue 72 type ACT_SITE sequence K description Nucleophile; Schiff-base intermediate with DNA; for 5'-dRP lyase activity => ECO:0000250|UniProtKB:P06746 source Swiss-Prot : SWS_FT_FI1 27) chain B residue 60 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P06746 source Swiss-Prot : SWS_FT_FI2 28) chain B residue 62 type BINDING sequence L description BINDING => ECO:0000250|UniProtKB:P06746 source Swiss-Prot : SWS_FT_FI2 29) chain B residue 65 type BINDING sequence V description BINDING => ECO:0000250|UniProtKB:P06746 source Swiss-Prot : SWS_FT_FI2 30) chain B residue 101 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P06746 source Swiss-Prot : SWS_FT_FI2 31) chain B residue 103 type BINDING sequence V description BINDING => ECO:0000250|UniProtKB:P06746 source Swiss-Prot : SWS_FT_FI2 32) chain B residue 106 type BINDING sequence I description BINDING => ECO:0000250|UniProtKB:P06746 source Swiss-Prot : SWS_FT_FI2 33) chain B residue 149 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P06746 source Swiss-Prot : SWS_FT_FI2 34) chain B residue 180 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:P06746 source Swiss-Prot : SWS_FT_FI2 35) chain B residue 183 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P06746 source Swiss-Prot : SWS_FT_FI2 36) chain B residue 189 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P06746 source Swiss-Prot : SWS_FT_FI2 37) chain B residue 190 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P06746 source Swiss-Prot : SWS_FT_FI2 38) chain B residue 192 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P06746 source Swiss-Prot : SWS_FT_FI2 39) chain B residue 256 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P06746 source Swiss-Prot : SWS_FT_FI2

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