|
|
eF-site ID
|
4bhp_18-A |
|
PDB Code
|
4bhp |
|
Model
|
18 |
|
Chain
|
A |
|
click to enlarge
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Title
|
A structural model of CAP mutant (T127L and S128I) in cGMP-bound state |
|
Classification
|
TRANSCRIPTION |
|
Compound
|
CAMP RECEPTOR PROTEIN |
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Source
|
Escherichia coli (strain K12) (CRP_ECOLI) |
|
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Sequence
|
A: |
VLGKPQTDPTLEWFLSHCHIHKYPSKSTLIHQGEKAETLY
YIVKGSVAVLIKDEEGKEMILSYLNQGDFIGELGLFEEGQ
ERSAWVRAKTACEVAEISYKKFRQLIQVNPDILMRLSAQM
ARRLQVLIEKVGNLAFLDVTGRIAQTLLNLAKQPDAMTHP
DGMQIKITRQEIGQIVGCSRETVGRILKMLEDQNLISAHG
KTIVVYGTR
|
|
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Description
|
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Functional site
|
|
|
1)
|
chain |
A |
| residue |
100 |
| type |
MOD_RES |
| sequence |
K
|
| description |
N6-acetyllysine => ECO:0000269|PubMed:18723842
|
| source |
Swiss-Prot : SWS_FT_FI5
|
|
|
2)
|
chain |
A |
| residue |
179-185 |
| type |
DNA_BIND |
| sequence |
SRETVGR
|
| description |
H-T-H motif => ECO:0000255|PROSITE-ProRule:PRU00387
|
| source |
Swiss-Prot : SWS_FT_FI1
|
|
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3)
|
chain |
A |
| residue |
167-190 |
| type |
prosite |
| sequence |
ITRQEIGQIVGCSRETVGRILKML
|
| description |
HTH_CRP_1 Crp-type HTH domain signature. ITRqeIGqIVGcSreTv.GRiLkmL
|
| source |
prosite : PS00042
|
|
|
4)
|
chain |
A |
| residue |
29-45 |
| type |
prosite |
| sequence |
LIHQGEKAETLYYIVKG
|
| description |
CNMP_BINDING_1 Cyclic nucleotide-binding domain signature 1. LIhQGEkAEtLYYIvkG
|
| source |
prosite : PS00888
|
|
|
5)
|
chain |
A |
| residue |
70-88 |
| type |
prosite |
| sequence |
IGELGLFEEGQERSAWVRA
|
| description |
CNMP_BINDING_2 Cyclic nucleotide-binding domain signature 2. IGElGLfeegqe.....RSAwVrA
|
| source |
prosite : PS00889
|
|
|
6)
|
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
|
|
|
7)
|
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
|
|
|
8)
|
chain |
A |
| residue |
127 |
| type |
BINDING |
| sequence |
L
|
| 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
|
|
|
9)
|
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
|
|
|
10)
|
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
|
|
|
11)
|
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
|
|
|
12)
|
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
|
|
|
13)
|
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
|
|
|
|