eF-site ID 5zod-A PDB Code 5zod Chain A click to enlarge Title Crystal Structure of hFen1 in apo form Classification HYDROLASE Compound Flap endonuclease 1 Source (FEN1_HUMAN) Sequence A:  GIQGLAKLIADVAPSAIRENDIKSYFGRKVAIDASMSHLM GMFYRTIRMMENGIKPVYVFDGKPPQNDECKHLLSLMGIP YLDAPSEAEASCAALVKAGKVYAAATEDMDCLTFGSPVLM RHLTASEAKKLPIQEFHLSRILQELGLNQEQFVDLCILLG SDYCESIRGIGPKRAVDLIQKHKSIEEIVRRLDPNKYPVP ENWLHKEAHQLFLEPEVLDPESVELKWSEPNEEELIKFMC GEKQFSEERIRSGVKRLSKS Description Functional site 1) chain A residue 160 type sequence E description binding site for residue MG A 402 source : AC2 2) chain A residue 179 type sequence D description binding site for residue MG A 402 source : AC2 3) chain A residue 181 type sequence D description binding site for residue MG A 402 source : AC2 4) chain A residue 233 type sequence D description binding site for residue MG A 402 source : AC2 5) chain A residue 234 type sequence Y description binding site for residue MG A 402 source : AC2 6) chain A residue 17 type sequence A description binding site for residue K A 403 source : AC3 7) chain A residue 19 type sequence R description binding site for residue K A 403 source : AC3 8) chain A residue 206 type sequence E description binding site for residue K A 403 source : AC3 9) chain A residue 208 type sequence H description binding site for residue K A 403 source : AC3 10) chain A residue 219 type sequence N description binding site for residue K A 404 source : AC4 11) chain A residue 220 type sequence Q description binding site for residue K A 404 source : AC4 12) chain A residue 221 type sequence E description binding site for residue K A 404 source : AC4 13) chain A residue 225 type sequence D description binding site for residue K A 405 source : AC5 14) chain A residue 276 type sequence H description binding site for residue K A 405 source : AC5 15) chain A residue 280 type sequence H description binding site for residue K A 405 source : AC5 16) chain A residue 289 type sequence L description binding site for residue K A 406 source : AC6 17) chain A residue 290 type sequence D description binding site for residue K A 406 source : AC6 18) chain A residue 291 type sequence P description binding site for residue K A 406 source : AC6 19) chain A residue 149-163 type prosite sequence GIPYLDAPSEAEASC description XPG_2 XPG protein signature 2. GIPYLdAPsEAEASC source prosite : PS00842 20) chain A residue 34 type BINDING sequence D description BINDING => ECO:0000269|PubMed:15616578, ECO:0007744|PDB:1UL1 source Swiss-Prot : SWS_FT_FI1 21) chain A residue 197 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:20068231 source Swiss-Prot : SWS_FT_FI10 22) chain A residue 255 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI11 23) chain A residue 293 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI11 24) chain A residue 70 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 25) chain A residue 231 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI2 26) 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 27) 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 28) 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 29) chain A residue 181 type BINDING sequence D description BINDING => ECO:0000269|PubMed:15616578, ECO:0007744|PDB:1UL1, ECO:0007744|PDB:5FV7, ECO:0007744|PDB:5ZOD source Swiss-Prot : SWS_FT_FI4 30) chain A residue 179 type BINDING sequence D description BINDING => ECO:0007744|PDB:5FV7, ECO:0007744|PDB:5ZOD source Swiss-Prot : SWS_FT_FI5 31) chain A residue 233 type BINDING sequence D description BINDING => ECO:0007744|PDB:5ZOD source Swiss-Prot : SWS_FT_FI6 32) 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 33) chain A residue 192 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 34) chain A residue 80 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI8 35) 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

Display surface Download Links