eF-site ID 3ber-A
PDB Code 3ber
Chain A

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Title Human DEAD-box RNA-helicase DDX47, conserved domain I in complex with AMP
Classification HYDROLASE
Compound Probable ATP-dependent RNA helicase DDX47
Source Homo sapiens (Human) (DDX47_HUMAN)
Sequence A:  TEASQPIVEEEETKTFKDLGVTDVLCEACDQLGWTKPTKI
QIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALLETP
QRLFALVLTPTRELAFQISEQFEALGSSIGVQSAVIVGGI
DSMSQSLALAKKPHIIIATPGRLIDHLENTKGFNLRALKY
LVMDEADRILNMDFETEVDKILKVIPRDRKTFLFSATMTK
KVQKLQRAALKNPVKCAVSS
Description


Functional site

1) chain A
residue 128
type
sequence G
description BINDING SITE FOR RESIDUE PO4 A 350
source : AC1

2) chain A
residue 129
type
sequence G
description BINDING SITE FOR RESIDUE PO4 A 350
source : AC1

3) chain A
residue 151
type
sequence G
description BINDING SITE FOR RESIDUE PO4 A 350
source : AC1

4) chain A
residue 152
type
sequence R
description BINDING SITE FOR RESIDUE PO4 A 350
source : AC1

5) chain A
residue 155
type
sequence D
description BINDING SITE FOR RESIDUE PO4 A 350
source : AC1

6) chain A
residue 26
type
sequence F
description BINDING SITE FOR RESIDUE AMP A 300
source : AC2

7) chain A
residue 44
type
sequence W
description BINDING SITE FOR RESIDUE AMP A 300
source : AC2

8) chain A
residue 46
type
sequence K
description BINDING SITE FOR RESIDUE AMP A 300
source : AC2

9) chain A
residue 51
type
sequence Q
description BINDING SITE FOR RESIDUE AMP A 300
source : AC2

10) chain A
residue 70
type
sequence T
description BINDING SITE FOR RESIDUE AMP A 300
source : AC2

11) chain A
residue 71
type
sequence G
description BINDING SITE FOR RESIDUE AMP A 300
source : AC2

12) chain A
residue 72
type
sequence S
description BINDING SITE FOR RESIDUE AMP A 300
source : AC2

13) chain A
residue 73
type
sequence G
description BINDING SITE FOR RESIDUE AMP A 300
source : AC2

14) chain A
residue 74
type
sequence K
description BINDING SITE FOR RESIDUE AMP A 300
source : AC2

15) chain A
residue 75
type
sequence T
description BINDING SITE FOR RESIDUE AMP A 300
source : AC2

16) chain A
residue 111
type
sequence Q
description BINDING SITE FOR RESIDUE AMP A 300
source : AC2

17) chain A
residue 155
type
sequence D
description BINDING SITE FOR RESIDUE PGE A 400
source : AC3

18) chain A
residue 155
type
sequence D
description BINDING SITE FOR RESIDUE PGE A 400
source : AC3

19) chain A
residue 156
type
sequence H
description BINDING SITE FOR RESIDUE PGE A 400
source : AC3

20) chain A
residue 156
type
sequence H
description BINDING SITE FOR RESIDUE PGE A 400
source : AC3

21) chain A
residue 159
type
sequence N
description BINDING SITE FOR RESIDUE PGE A 400
source : AC3

22) chain A
residue 159
type
sequence N
description BINDING SITE FOR RESIDUE PGE A 400
source : AC3

23) chain A
residue 160
type
sequence T
description BINDING SITE FOR RESIDUE PGE A 400
source : AC3

24) chain A
residue 160
type
sequence T
description BINDING SITE FOR RESIDUE PGE A 400
source : AC3

25) chain A
residue 18
type
sequence V
description BINDING SITE FOR RESIDUE PGE A 401
source : AC4

26) chain A
residue 192
type
sequence L
description BINDING SITE FOR RESIDUE PGE A 401
source : AC4

27) chain A
residue 197
type
sequence R
description BINDING SITE FOR RESIDUE PGE A 401
source : AC4

28) chain A
residue 199
type
sequence R
description BINDING SITE FOR RESIDUE PGE A 401
source : AC4

29) chain A
residue 217
type
sequence R
description BINDING SITE FOR RESIDUE PGE A 401
source : AC4

30) chain A
residue 218
type
sequence A
description BINDING SITE FOR RESIDUE PGE A 401
source : AC4

31) chain A
residue 219
type
sequence A
description BINDING SITE FOR RESIDUE PGE A 401
source : AC4

32) chain A
residue 220
type
sequence L
description BINDING SITE FOR RESIDUE PGE A 401
source : AC4

33) chain A
residue 172-180
type prosite
sequence VMDEADRIL
description DEAD_ATP_HELICASE DEAD-box subfamily ATP-dependent helicases signature. VMDEADRiL
source prosite : PS00039

34) chain A
residue 68
type BINDING
sequence A
description
source Swiss-Prot : SWS_FT_FI1

35) chain A
residue 149
type MOD_RES
sequence T
description Phosphothreonine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI3


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