eF-site ID 1u20-AB
PDB Code 1u20
Chain A, B

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Title Crystal Structure of Xenopus laevis nudix hydrolase nuclear SnoRNA decapping Protein X29
Classification HYDROLASE
Compound U8 snoRNA-binding protein X29
Source Xenopus laevis (African clawed frog) (Q6TEC1_XENLA)
Sequence A:  DKPRPRNISREESLQLEGYKHACHALLHAPSQAKLFDRVP
IRRVLLMMMRFDGRLGFPGGFVDTRDISLEEGLKRELEEE
LGPALATVEVTEDDYRSSQVREHPQKCVTHFYIKELKLEE
IERIEAEAVNAKDHGLEVMGLIRVPLYTLRDRVGGLPAFL
CNNFIGNSKSQLLYALRSLKLLREDQIQEVLKASHR
B:  PRNISREESLQLEGYKHACHALLHAPSQAKLFDRVPIRRV
LLMMMRFDGRLGFPGGFVDTRDISLEEGLKRELEEELGPA
LATVEVTEDDYRSSQVREHPQKCVTHFYIKELKLEEIERI
EAEAVNAKDHGLEVMGLIRVPLYTLRDRVGGLPAFLCNNF
IGNSKSQLLYALRSLKLLREDQIQEVLKASHR
Description


Functional site

1) chain A
residue 132
type
sequence E
description BINDING SITE FOR RESIDUE GOL A 500
source : AC1

2) chain A
residue 135
type
sequence E
description BINDING SITE FOR RESIDUE GOL A 500
source : AC1

3) chain A
residue 163
type
sequence R
description BINDING SITE FOR RESIDUE GOL A 500
source : AC1

4) chain B
residue 37
type
sequence H
description BINDING SITE FOR RESIDUE GOL B 501
source : AC2

5) chain B
residue 63
type
sequence R
description BINDING SITE FOR RESIDUE GOL B 501
source : AC2

6) chain A
residue 37
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:16472752
source Swiss-Prot : SWS_FT_FI1

7) chain B
residue 63
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:16472752
source Swiss-Prot : SWS_FT_FI1

8) chain B
residue 72
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:16472752
source Swiss-Prot : SWS_FT_FI1

9) chain B
residue 89
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:16472752
source Swiss-Prot : SWS_FT_FI1

10) chain B
residue 93
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:16472752
source Swiss-Prot : SWS_FT_FI1

11) chain B
residue 150
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:16472752
source Swiss-Prot : SWS_FT_FI1

12) chain B
residue 180
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:16472752
source Swiss-Prot : SWS_FT_FI1

13) chain B
residue 184
type BINDING
sequence Q
description BINDING => ECO:0000269|PubMed:16472752
source Swiss-Prot : SWS_FT_FI1

14) chain A
residue 63
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:16472752
source Swiss-Prot : SWS_FT_FI1

15) chain A
residue 72
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:16472752
source Swiss-Prot : SWS_FT_FI1

16) chain A
residue 89
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:16472752
source Swiss-Prot : SWS_FT_FI1

17) chain A
residue 93
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:16472752
source Swiss-Prot : SWS_FT_FI1

18) chain A
residue 150
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:16472752
source Swiss-Prot : SWS_FT_FI1

19) chain A
residue 180
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:16472752
source Swiss-Prot : SWS_FT_FI1

20) chain A
residue 184
type BINDING
sequence Q
description BINDING => ECO:0000269|PubMed:16472752
source Swiss-Prot : SWS_FT_FI1

21) chain B
residue 37
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:16472752
source Swiss-Prot : SWS_FT_FI1

22) chain A
residue 70
type BINDING
sequence F
description BINDING => ECO:0000250|UniProtKB:Q96DE0
source Swiss-Prot : SWS_FT_FI2

23) chain B
residue 70
type BINDING
sequence F
description BINDING => ECO:0000250|UniProtKB:Q96DE0
source Swiss-Prot : SWS_FT_FI2


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