eF-site ID 3q8k-A PDB Code 3q8k Chain A click to enlarge Title Crystal Structure of Human Flap Endonuclease FEN1 (WT) in complex with product 5'-flap DNA, SM3+, and K+ Classification HYDROLASE/DNA Compound Flap endonuclease 1 Source Homo sapiens (Human) (3Q8K) Sequence A:  GIQGLAKLIADVAPSAIRENDIKSYFGRKVAIDASMSIYQ FLIAVRQGGDVLQNEEGETTSHLMGMFYRTIRMMENGIKP VYVFDGKPPQLKSGELAKRSERRAEAEKQLQQAQAAGAEQ EVEKFTKRLVKVTKQHNDECKHLLSLMGIPYLDAPSEAEA SCAALVKAGKVYAAATEDMDCLTFGSPVLMRHLTASEAKK LPIQEFHLSRILQELGLNQEQFVDLCILLGSDYCESIRGI GPKRAVDLIQKHKSIEEIVRRLDPNKYPVPENWLHKEAHQ LFLEPEVLDPESVELKWSEPNEEELIKFMCGEKQFSEERI RSGVKRLSKSRQGSTLEVLFQ Description Functional site 1) chain A residue 86 type sequence D description BINDING SITE FOR RESIDUE SM A 1001 source : AC1 2) chain A residue 160 type sequence E description BINDING SITE FOR RESIDUE SM A 1001 source : AC1 3) chain A residue 160 type sequence E description BINDING SITE FOR RESIDUE SM A 1002 source : AC2 4) chain A residue 179 type sequence D description BINDING SITE FOR RESIDUE SM A 1002 source : AC2 5) chain A residue 181 type sequence D description BINDING SITE FOR RESIDUE SM A 1002 source : AC2 6) chain A residue 57 type sequence E description BINDING SITE FOR RESIDUE SM A 1003 source : AC3 7) chain A residue 285 type sequence E description BINDING SITE FOR RESIDUE SM A 1003 source : AC3 8) chain A residue 313 type sequence E description BINDING SITE FOR RESIDUE SM A 1003 source : AC3 9) chain A residue 342 type sequence Q description BINDING SITE FOR RESIDUE SM A 1003 source : AC3 10) chain A residue 57 type sequence E description BINDING SITE FOR RESIDUE SM A 1004 source : AC4 11) chain A residue 59 type sequence E description BINDING SITE FOR RESIDUE SM A 1004 source : AC4 12) chain A residue 313 type sequence E description BINDING SITE FOR RESIDUE SM A 1004 source : AC4 13) chain A residue 342 type sequence Q description BINDING SITE FOR RESIDUE SM A 1004 source : AC4 14) chain A residue 237 type sequence S description BINDING SITE FOR RESIDUE K A 1101 source : AC5 15) chain A residue 238 type sequence I description BINDING SITE FOR RESIDUE K A 1101 source : AC5 16) chain A residue 241 type sequence I description BINDING SITE FOR RESIDUE K A 1101 source : AC5 17) chain A residue 2 type sequence G description BINDING SITE FOR RESIDUE OH A 347 source : AC6 18) chain A residue 179 type sequence D description BINDING SITE FOR RESIDUE OH A 347 source : AC6 19) chain A residue 181 type sequence D description BINDING SITE FOR RESIDUE OH A 347 source : AC6 20) chain A residue 233 type sequence D description BINDING SITE FOR RESIDUE OH A 347 source : AC6 21) 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 22) 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 23) chain A residue 179 type BINDING sequence D description BINDING => ECO:0007744|PDB:5FV7, ECO:0007744|PDB:5ZOD source Swiss-Prot : SWS_FT_FI5 24) chain A residue 233 type BINDING sequence D description BINDING => ECO:0007744|PDB:5ZOD source Swiss-Prot : SWS_FT_FI6 25) chain A residue 197 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:20068231 source Swiss-Prot : SWS_FT_FI10 26) chain A residue 255 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI11 27) chain A residue 293 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI11 28) chain A residue 335 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI11 29) chain A residue 336 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI12 30) chain A residue 47 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 31) chain A residue 70 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 32) chain A residue 231 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI2 33) 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 34) 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 35) 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 36) chain A residue 100 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 37) chain A residue 104 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 38) 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 39) chain A residue 80 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI8 40) 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 41) chain A residue 34 type BINDING sequence D description BINDING => ECO:0000269|PubMed:15616578, ECO:0007744|PDB:1UL1 source Swiss-Prot : SWS_FT_FI1 42) chain A residue 79-93 type prosite sequence IKPVYVFDGKPPQLK description XPG_1 XPG protein signature 1. IKPvYVFDGkpPqLK source prosite : PS00841 43) chain A residue 149-163 type prosite sequence GIPYLDAPSEAEASC description XPG_2 XPG protein signature 2. GIPYLdAPsEAEASC source prosite : PS00842

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