eF-site ID 6n6i-AB
PDB Code 6n6i
Chain A, B

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Title Human REXO2 bound to pGG
Classification rna binding protein/rna
Compound RNA exonuclease 2 homolog,Small fragment nuclease
Source (6N6I)
Sequence A:  GESMAQRMVWVDLEMTGLDIEKDQIIEMACLITDSDLNIL
AEGPNLIIKQPDELLDSMSDWCKEHHGKSGLTKAVKESTI
TLQQAEYEFLSFVRQQTPPGLCPLAGNSVHEDKKFLDKYM
PQFMKHLHYRIIDVSTVKELCRRWYPEEYEFAPKKAASHR
ALDDISESIKELQFYRNNIFKKK
B:  AAGESMAQRMVWVDLEMTGLDIEKDQIIEMACLITDSDLN
ILAEGPNLIIKQPDELLDSMSDWCKEHHGKSGLTKAVKES
TITLQQAEYEFLSFVRQQTPPGLCPLAGNSVHEDKKFLDK
YMPQFMKHLHYRIIDVSTVKELCRRWYPEEYEFAPKKAAS
HRALDDISESIKELQFYRNNIFKKKI
Description


Functional site

1) chain A
residue 110
type
sequence N
description binding site for residue GOL A 301
source : AC1

2) chain A
residue 158
type
sequence K
description binding site for residue GOL A 301
source : AC1

3) chain A
residue 160
type
sequence A
description binding site for residue GOL A 301
source : AC1

4) chain A
residue 162
type
sequence H
description binding site for residue GOL A 301
source : AC1

5) chain A
residue 167
type
sequence D
description binding site for residue GOL A 301
source : AC1

6) chain A
residue 15
type
sequence D
description binding site for residue NA D 701
source : AC2

7) chain A
residue 86
type
sequence Q
description binding site for residue GOL B 301
source : AC3

8) chain A
residue 89
type
sequence E
description binding site for residue GOL B 301
source : AC3

9) chain A
residue 124
type
sequence P
description binding site for residue GOL B 301
source : AC3

10) chain A
residue 125
type
sequence Q
description binding site for residue GOL B 301
source : AC3

11) chain B
residue 45
type
sequence E
description binding site for residue GOL B 301
source : AC3

12) chain B
residue 169
type
sequence S
description binding site for residue GOL B 301
source : AC3

13) chain A
residue 186
type
sequence K
description binding site for residue MLI B 302
source : AC4

14) chain B
residue 97
type
sequence R
description binding site for residue MLI B 302
source : AC4

15) chain B
residue 102
type
sequence P
description binding site for residue MLI B 302
source : AC4

16) chain B
residue 151
type
sequence E
description binding site for residue MLI B 302
source : AC4

17) chain B
residue 110
type
sequence N
description binding site for residue EDO C 701
source : AC5

18) chain B
residue 167
type
sequence D
description binding site for residue EDO C 701
source : AC5

19) chain B
residue 15
type
sequence D
description binding site for residue NA C 702
source : AC6

20) chain A
residue 173
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:Q9D8S4
source Swiss-Prot : SWS_FT_FI8

21) chain B
residue 173
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:Q9D8S4
source Swiss-Prot : SWS_FT_FI8

22) chain B
residue 47
type BINDING
sequence P
description BINDING => ECO:0000269|PubMed:30926754, ECO:0000269|PubMed:31588022, ECO:0007744|PDB:6J7Y, ECO:0007744|PDB:6RCN
source Swiss-Prot : SWS_FT_FI2

23) chain B
residue 49
type BINDING
sequence L
description BINDING => ECO:0000269|PubMed:30926754, ECO:0000269|PubMed:31588022, ECO:0007744|PDB:6J7Y, ECO:0007744|PDB:6RCN
source Swiss-Prot : SWS_FT_FI2

24) chain A
residue 47
type BINDING
sequence P
description BINDING => ECO:0000269|PubMed:30926754, ECO:0000269|PubMed:31588022, ECO:0007744|PDB:6J7Y, ECO:0007744|PDB:6RCN
source Swiss-Prot : SWS_FT_FI2

25) chain A
residue 49
type BINDING
sequence L
description BINDING => ECO:0000269|PubMed:30926754, ECO:0000269|PubMed:31588022, ECO:0007744|PDB:6J7Y, ECO:0007744|PDB:6RCN
source Swiss-Prot : SWS_FT_FI2

26) chain A
residue 147
type BINDING
sequence W
description BINDING => ECO:0000269|PubMed:30926754, ECO:0000269|PubMed:31588022, ECO:0007744|PDB:6RCN
source Swiss-Prot : SWS_FT_FI3

27) chain B
residue 147
type BINDING
sequence W
description BINDING => ECO:0000269|PubMed:30926754, ECO:0000269|PubMed:31588022, ECO:0007744|PDB:6RCN
source Swiss-Prot : SWS_FT_FI3

28) chain A
residue 164
type SITE
sequence A
description Important for dinucleotide binding => ECO:0000269|PubMed:30926754, ECO:0000269|PubMed:32365187
source Swiss-Prot : SWS_FT_FI5

29) chain B
residue 53
type SITE
sequence Q
description Important for dinucleotide binding => ECO:0000269|PubMed:30926754, ECO:0000269|PubMed:32365187
source Swiss-Prot : SWS_FT_FI5

30) chain B
residue 96
type SITE
sequence V
description Important for dinucleotide binding => ECO:0000269|PubMed:30926754, ECO:0000269|PubMed:32365187
source Swiss-Prot : SWS_FT_FI5

31) chain B
residue 164
type SITE
sequence A
description Important for dinucleotide binding => ECO:0000269|PubMed:30926754, ECO:0000269|PubMed:32365187
source Swiss-Prot : SWS_FT_FI5

32) chain A
residue 53
type SITE
sequence Q
description Important for dinucleotide binding => ECO:0000269|PubMed:30926754, ECO:0000269|PubMed:32365187
source Swiss-Prot : SWS_FT_FI5

33) chain A
residue 96
type SITE
sequence V
description Important for dinucleotide binding => ECO:0000269|PubMed:30926754, ECO:0000269|PubMed:32365187
source Swiss-Prot : SWS_FT_FI5

34) chain A
residue 92
type MOD_RES
sequence F
description Phosphoserine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI6

35) chain B
residue 92
type MOD_RES
sequence F
description Phosphoserine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI6

36) chain A
residue 122
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0007744|PubMed:15592455
source Swiss-Prot : SWS_FT_FI7

37) chain B
residue 122
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0007744|PubMed:15592455
source Swiss-Prot : SWS_FT_FI7


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