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

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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


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