eF-site ID 1o3s-A
PDB Code 1o3s
Chain A

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Title PROTEIN-DNA RECOGNITION AND DNA DEFORMATION REVEALED IN CRYSTAL STRUCTURES OF CAP-DNA COMPLEXES
Classification GENE REGULATION/DNA
Compound 5'-D(*AP*AP*AP*AP*AP*TP*GP*CP*GP*AP*T)-3'
Source Escherichia coli (strain K12) (1O3S)
Sequence A:  DPTLEWFLSHCHIHKYPSKSTLIHQGEKAETLYYIVKGSV
AVLIKDEEGKEMILSYLNQGDFIGELGLFEEGQERSAWVR
AKTACEVAEISYKKFRQLIQVNPDILMRLSAQMARRLQVT
SEKVGNLAFLDVTGRIAQTLLNLAKQPDAMTHPDGMQIKI
TRQEIGQIVGCSRDTVGRILKMLEDQNLISAHGKTIVVYG
Description


Functional site

1) chain A
residue 49
type
sequence V
description BINDING SITE FOR RESIDUE CMP A 1
source : AC1

2) chain A
residue 61
type
sequence L
description BINDING SITE FOR RESIDUE CMP A 1
source : AC1

3) chain A
residue 70
type
sequence I
description BINDING SITE FOR RESIDUE CMP A 1
source : AC1

4) chain A
residue 71
type
sequence G
description BINDING SITE FOR RESIDUE CMP A 1
source : AC1

5) chain A
residue 72
type
sequence E
description BINDING SITE FOR RESIDUE CMP A 1
source : AC1

6) chain A
residue 73
type
sequence L
description BINDING SITE FOR RESIDUE CMP A 1
source : AC1

7) chain A
residue 82
type
sequence R
description BINDING SITE FOR RESIDUE CMP A 1
source : AC1

8) chain A
residue 83
type
sequence S
description BINDING SITE FOR RESIDUE CMP A 1
source : AC1

9) chain A
residue 123
type
sequence R
description BINDING SITE FOR RESIDUE CMP A 1
source : AC1

10) chain A
residue 127
type
sequence T
description BINDING SITE FOR RESIDUE CMP A 1
source : AC1

11) chain A
residue 128
type
sequence S
description BINDING SITE FOR RESIDUE CMP A 1
source : AC1

12) chain A
residue 57
type
sequence K
description BINDING SITE FOR RESIDUE CMP A 2
source : AC2

13) chain A
residue 58
type
sequence E
description BINDING SITE FOR RESIDUE CMP A 2
source : AC2

14) chain A
residue 135
type
sequence A
description BINDING SITE FOR RESIDUE CMP A 2
source : AC2

15) chain A
residue 136
type
sequence F
description BINDING SITE FOR RESIDUE CMP A 2
source : AC2

16) chain A
residue 170
type
sequence Q
description BINDING SITE FOR RESIDUE CMP A 2
source : AC2

17) chain A
residue 173
type
sequence G
description BINDING SITE FOR RESIDUE CMP A 2
source : AC2

18) chain A
residue 174
type
sequence Q
description BINDING SITE FOR RESIDUE CMP A 2
source : AC2

19) chain A
residue 178
type
sequence C
description BINDING SITE FOR RESIDUE CMP A 2
source : AC2

20) chain A
residue 179
type
sequence S
description BINDING SITE FOR RESIDUE CMP A 2
source : AC2

21) chain A
residue 180
type
sequence R
description BINDING SITE FOR RESIDUE CMP A 2
source : AC2

22) chain A
residue 167-190
type prosite
sequence ITRQEIGQIVGCSRDTVGRILKML
description HTH_CRP_1 Crp-type HTH domain signature. ITRqeIGqIVGcSrdTv.GRiLkmL
source prosite : PS00042

23) chain A
residue 29-45
type prosite
sequence LIHQGEKAETLYYIVKG
description CNMP_BINDING_1 Cyclic nucleotide-binding domain signature 1. LIhQGEkAEtLYYIvkG
source prosite : PS00888

24) chain A
residue 70-88
type prosite
sequence IGELGLFEEGQERSAWVRA
description CNMP_BINDING_2 Cyclic nucleotide-binding domain signature 2. IGElGLfeegqe.....RSAwVrA
source prosite : PS00889

25) chain A
residue 179-185
type DNA_BIND
sequence SRDTVGR
description H-T-H motif => ECO:0000255|PROSITE-ProRule:PRU00387
source Swiss-Prot : SWS_FT_FI1

26) chain A
residue 56
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:11124031, ECO:0000269|PubMed:12202833, ECO:0000269|PubMed:1653449, ECO:0000269|PubMed:2828639, ECO:0000269|PubMed:6286624, ECO:0000269|PubMed:8757802
source Swiss-Prot : SWS_FT_FI2

27) chain A
residue 71
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:11124031, ECO:0000269|PubMed:12202833, ECO:0000269|PubMed:1653449, ECO:0000269|PubMed:2828639, ECO:0000269|PubMed:6286624, ECO:0000269|PubMed:8757802
source Swiss-Prot : SWS_FT_FI2

28) chain A
residue 82
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:11124031, ECO:0000269|PubMed:12202833, ECO:0000269|PubMed:1653449, ECO:0000269|PubMed:2828639, ECO:0000269|PubMed:6286624, ECO:0000269|PubMed:8757802
source Swiss-Prot : SWS_FT_FI2

29) chain A
residue 127
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:11124031, ECO:0000269|PubMed:12202833, ECO:0000269|PubMed:1653449, ECO:0000269|PubMed:2828639, ECO:0000269|PubMed:6286624, ECO:0000269|PubMed:8757802
source Swiss-Prot : SWS_FT_FI2

30) chain A
residue 135
type BINDING
sequence A
description BINDING => ECO:0000269|PubMed:11124031, ECO:0000269|PubMed:12202833, ECO:0000269|PubMed:1653449, ECO:0000269|PubMed:2828639, ECO:0000269|PubMed:6286624, ECO:0000269|PubMed:8757802
source Swiss-Prot : SWS_FT_FI2

31) chain A
residue 170
type BINDING
sequence Q
description BINDING => ECO:0000269|PubMed:11124031, ECO:0000269|PubMed:12202833, ECO:0000269|PubMed:1653449, ECO:0000269|PubMed:2828639, ECO:0000269|PubMed:6286624, ECO:0000269|PubMed:8757802
source Swiss-Prot : SWS_FT_FI2

32) chain A
residue 96
type SITE
sequence E
description Activating region 2 (AR2); probably contacts the N-terminus of RpoA => ECO:0000269|PubMed:8978616
source Swiss-Prot : SWS_FT_FI3

33) chain A
residue 101
type SITE
sequence K
description Activating region 2 (AR2); probably contacts the N-terminus of RpoA => ECO:0000269|PubMed:15520470, ECO:0000269|PubMed:8978616
source Swiss-Prot : SWS_FT_FI4

34) chain A
residue 100
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000269|PubMed:18723842
source Swiss-Prot : SWS_FT_FI5


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