eF-site ID 5k97-A
PDB Code 5k97
Chain A

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Title Flap endonuclease 1 (FEN1) D233N with cleaved product fragment and Sm3+
Classification HYDROLASE/DNA
Compound Flap endonuclease 1
Source (5K97)
Sequence A:  GIQGLAKLIADVAPSAIRENDIKSYFGRKVAIDASMSIYQ
FLIAVRQGGDVLQNEEGETTSHLMGMFYRTIRMMENGIKP
VYVFDGKPPQLKSGELAKRSERRAEAEKQLQQAQAAGAEQ
EVEKFTKRLVKVTKQHNDECKHLLSLMGIPYLDAPSEAEA
SCAALVKAGKVYAAATEDMDCLTFGSPVLMRHLTASEAKK
LPIQEFHLSRILQELGLNQEQFVDLCILLGSNYCESIRGI
GPKRAVDLIQKHKSIEEIVRRLDPNKYPVPENWLHKEAHQ
LFLEPEVLDPESVELKWSEPNEEELIKFMCGEKQFSEERI
RSGVKRLSKSRQGSTLEVLFQ
Description


Functional site

1) chain A
residue 2
type
sequence G
description binding site for residue SM A 401
source : AC1

2) chain A
residue 160
type
sequence E
description binding site for residue SM A 401
source : AC1

3) chain A
residue 181
type
sequence D
description binding site for residue SM A 401
source : AC1

4) chain A
residue 86
type
sequence D
description binding site for residue SM A 402
source : AC2

5) chain A
residue 158
type
sequence E
description binding site for residue SM A 402
source : AC2

6) chain A
residue 160
type
sequence E
description binding site for residue SM A 402
source : AC2

7) chain A
residue 160
type
sequence E
description binding site for residue SM A 403
source : AC3

8) chain A
residue 179
type
sequence D
description binding site for residue SM A 403
source : AC3

9) chain A
residue 181
type
sequence D
description binding site for residue SM A 403
source : AC3

10) chain A
residue 158
type
sequence E
description binding site for residue SM A 404
source : AC4

11) chain A
residue 160
type
sequence E
description binding site for residue SM A 404
source : AC4

12) chain A
residue 237
type
sequence S
description binding site for residue K A 405
source : AC5

13) chain A
residue 238
type
sequence I
description binding site for residue K A 405
source : AC5

14) chain A
residue 241
type
sequence I
description binding site for residue K A 405
source : AC5

15) chain A
residue 57
type
sequence E
description binding site for residue SM A 406
source : AC6

16) chain A
residue 285
type
sequence E
description binding site for residue SM A 406
source : AC6

17) chain A
residue 313
type
sequence E
description binding site for residue SM A 406
source : AC6

18) chain A
residue 342
type
sequence Q
description binding site for residue SM A 406
source : AC6

19) chain A
residue 57
type
sequence E
description binding site for residue SM A 407
source : AC7

20) chain A
residue 59
type
sequence E
description binding site for residue SM A 407
source : AC7

21) chain A
residue 313
type
sequence E
description binding site for residue SM A 407
source : AC7

22) chain A
residue 342
type
sequence Q
description binding site for residue SM A 407
source : AC7

23) chain A
residue 49
type
sequence G
description binding site for residue SM A 408
source : AC8

24) chain A
residue 51
type
sequence D
description binding site for residue SM A 408
source : AC8

25) chain A
residue 102
type
sequence E
description binding site for residue SM A 409
source : AC9

26) chain A
residue 2
type
sequence G
description binding site for residue EDO A 410
source : AD1

27) chain A
residue 3
type
sequence I
description binding site for residue EDO A 410
source : AD1

28) chain A
residue 179
type
sequence D
description binding site for residue EDO A 410
source : AD1

29) chain A
residue 180
type
sequence M
description binding site for residue EDO A 410
source : AD1

30) 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

31) 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

32) 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

33) 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

34) chain A
residue 179
type BINDING
sequence D
description BINDING => ECO:0007744|PDB:5FV7, ECO:0007744|PDB:5ZOD
source Swiss-Prot : SWS_FT_FI5

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 79-93
type prosite
sequence IKPVYVFDGKPPQLK
description XPG_1 XPG protein signature 1. IKPvYVFDGkpPqLK
source prosite : PS00841

41) chain A
residue 149-163
type prosite
sequence GIPYLDAPSEAEASC
description XPG_2 XPG protein signature 2. GIPYLdAPsEAEASC
source prosite : PS00842

42) chain A
residue 34
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:15616578, ECO:0007744|PDB:1UL1
source Swiss-Prot : SWS_FT_FI1

43) chain A
residue 197
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:20068231
source Swiss-Prot : SWS_FT_FI10

44) chain A
residue 255
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI11

45) chain A
residue 293
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI11

46) chain A
residue 335
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI11

47) chain A
residue 336
type MOD_RES
sequence T
description Phosphothreonine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI12

48) chain A
residue 47
type BINDING
sequence R
description
source Swiss-Prot : SWS_FT_FI2

49) chain A
residue 70
type BINDING
sequence R
description
source Swiss-Prot : SWS_FT_FI2

50) chain A
residue 231
type BINDING
sequence G
description
source Swiss-Prot : SWS_FT_FI2

51) 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

52) chain A
residue 233
type BINDING
sequence N
description BINDING => ECO:0007744|PDB:5ZOD
source Swiss-Prot : SWS_FT_FI6


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