eF-site ID 5zof-A PDB Code 5zof Chain A click to enlarge Title Crystal Structure of D181A/R192F hFen1 in complex with DNA Classification HYDROLASE/DNA Compound Flap endonuclease 1 Source (5ZOF) Sequence A:  GIQGLAKLIADVAPSAIRENDIKSYFGRKVAIDASMSIYQ FLIAVRQGGDVLQNEEGETTSHLMGMFYRTIRMMENGIKP VYVFDGKVKVTKQHNDECKHLLSLMGIPYLDAPSEAEASC AALVKAGKVYAAATEDMACLTFGSPVLMFHLTASEAKKLP IQEFHLSRILQELGLNQEQFVDLCILLGSDYCESIRGIGP KRAVDLIQKHKSIEEIVRRLDPNKYPVPENWLHKEAHQLF LEPEVLDPESVELKWSEPNEEELIKFMCGEKQFSEERIRS GVKRLSKSRQ Description Functional site 1) chain A residue 237 type sequence S description binding site for residue K A 401 source : AC1 2) chain A residue 238 type sequence I description binding site for residue K A 401 source : AC1 3) chain A residue 241 type sequence I description binding site for residue K A 401 source : AC1 4) chain A residue 34 type BINDING sequence D description BINDING => ECO:0000269|PubMed:15616578, ECO:0007744|PDB:1UL1 source Swiss-Prot : SWS_FT_FI1 5) chain A residue 47 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 6) chain A residue 70 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 7) chain A residue 231 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI2 8) chain A residue 86 type BINDING sequence D description BINDING => ECO:0000269|PubMed:15616578, ECO:0007744|PDB:1UL1, ECO:0007744|PDB:5FV7 source Swiss-Prot : SWS_FT_FI3 9) chain A residue 158 type BINDING sequence E description BINDING => ECO:0000269|PubMed:15616578, ECO:0007744|PDB:1UL1, ECO:0007744|PDB:5FV7 source Swiss-Prot : SWS_FT_FI3 10) chain A residue 160 type BINDING sequence E description BINDING => ECO:0000269|PubMed:15616578, ECO:0007744|PDB:1UL1, ECO:0007744|PDB:5FV7, ECO:0007744|PDB:5ZOD source Swiss-Prot : SWS_FT_FI4 11) chain A residue 181 type BINDING sequence A description BINDING => ECO:0000269|PubMed:15616578, ECO:0007744|PDB:1UL1, ECO:0007744|PDB:5FV7, ECO:0007744|PDB:5ZOD source Swiss-Prot : SWS_FT_FI4 12) chain A residue 233 type BINDING sequence D description BINDING => ECO:0007744|PDB:5ZOD source Swiss-Prot : SWS_FT_FI6 13) chain A residue 197 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:20068231 source Swiss-Prot : SWS_FT_FI10 14) chain A residue 255 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI11 15) chain A residue 293 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI11 16) chain A residue 179 type BINDING sequence D description BINDING => ECO:0007744|PDB:5FV7, ECO:0007744|PDB:5ZOD source Swiss-Prot : SWS_FT_FI5 17) chain A residue 19 type MOD_RES sequence R description Symmetric dimethylarginine; by PRMT5 => ECO:0000255|HAMAP-Rule:MF_03140, ECO:0000269|PubMed:20729856 source Swiss-Prot : SWS_FT_FI7 18) chain A residue 192 type MOD_RES sequence F description Symmetric dimethylarginine; by PRMT5 => ECO:0000255|HAMAP-Rule:MF_03140, ECO:0000269|PubMed:20729856 source Swiss-Prot : SWS_FT_FI7 19) chain A residue 80 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI8 20) chain A residue 187 type MOD_RES sequence S description Phosphoserine; by CDK2 => ECO:0000255|HAMAP-Rule:MF_03140, ECO:0000269|PubMed:20729856 source Swiss-Prot : SWS_FT_FI9 21) chain A residue 149-163 type prosite sequence GIPYLDAPSEAEASC description XPG_2 XPG protein signature 2. GIPYLdAPsEAEASC source prosite : PS00842

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