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

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Title Crystal structure of the DEAD domain of Human eIF4A with sanguinarine
Classification HYDROLASE
Compound Eukaryotic initiation factor 4A-I
Source (IF4A1_HUMAN)
Sequence A:  GVIESNWNEIVDSFDDMNLSESLLRGIYAYGFEXPSAIQQ
RAILPCIXGYDVIAQAQSGTGXTATFAISILQQIELDLXA
TQALVLAPTRELAQQIQXVVMALGDYMGASCHACIGGTNV
RAEVQXLQMEAPHIIVGTPGRVFDMLNRRYLSPXYIXMFV
LDEADEMLSRGFXDQIYDIFQXLNSNTQVVLLSATMPSDV
LEVTXXFMRDPIRILVXX
Description


Functional site

1) chain A
residue 50
type
sequence Y
description binding site for residue SAU A 301
source : AC1

2) chain A
residue 50
type
sequence Y
description binding site for residue SAU A 301
source : AC1

3) chain A
residue 51
type
sequence G
description binding site for residue SAU A 301
source : AC1

4) chain A
residue 52
type
sequence F
description binding site for residue SAU A 301
source : AC1

5) chain A
residue 79
type
sequence G
description binding site for residue SAU A 301
source : AC1

6) chain A
residue 80
type
sequence T
description binding site for residue SAU A 301
source : AC1

7) chain A
residue 81
type
sequence G
description binding site for residue SAU A 301
source : AC1

8) chain A
residue 115
type
sequence Q
description binding site for residue SAU A 301
source : AC1

9) chain A
residue 78
type
sequence S
description binding site for residue MLI A 302
source : AC2

10) chain A
residue 79
type
sequence G
description binding site for residue MLI A 302
source : AC2

11) chain A
residue 80
type
sequence T
description binding site for residue MLI A 302
source : AC2

12) chain A
residue 81
type
sequence G
description binding site for residue MLI A 302
source : AC2

13) chain A
residue 82
type
sequence X
description binding site for residue MLI A 302
source : AC2

14) chain A
residue 83
type
sequence T
description binding site for residue MLI A 302
source : AC2

15) chain A
residue 115
type
sequence Q
description binding site for residue MLI A 302
source : AC2

16) chain A
residue 180-188
type prosite
sequence VLDEADEML
description DEAD_ATP_HELICASE DEAD-box subfamily ATP-dependent helicases signature. VLDEADEmL
source prosite : PS00039

17) chain A
residue 76
type BINDING
sequence A
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00541
source Swiss-Prot : SWS_FT_FI1

18) chain A
residue 118
type MOD_RES
sequence X
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI2

19) chain A
residue 174
type MOD_RES
sequence X
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI2

20) chain A
residue 158
type MOD_RES
sequence T
description Phosphothreonine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI3

21) chain A
residue 193
type MOD_RES
sequence X
description N6-acetyllysine => ECO:0000250|UniProtKB:P60843
source Swiss-Prot : SWS_FT_FI4

22) chain A
residue 238
type MOD_RES
sequence X
description N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P60843
source Swiss-Prot : SWS_FT_FI5

23) chain A
residue 146
type CROSSLNK
sequence X
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
source Swiss-Prot : SWS_FT_FI6

24) chain A
residue 225
type CROSSLNK
sequence X
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
source Swiss-Prot : SWS_FT_FI6

25) chain A
residue 238
type CROSSLNK
sequence X
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733
source Swiss-Prot : SWS_FT_FI7


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