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eF-site ID
|
3pcs-ABCDEFGH |
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PDB Code
|
3pcs |
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Chain
|
A, B, C, D, E, F, G, H |
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click to enlarge
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Title
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Structure of EspG-PAK2 autoinhibitory Ialpha3 helix complex |
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Classification
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PROTEIN TRANSPORT/TRANSFERASE |
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Compound
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EspG |
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Source
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null (PAK2_HUMAN) |
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Sequence
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A: |
KKSWDEMSCAEKLFKVLSFGLWNPTYSRSERQSFQELLTV
LEPVYPLPNELGRVSARFSDGSSLRISVTNSELVEAEIRT
ANNEKITVLLESNEQNRLLQSLPIDRHMPYIQVHRALLTD
TTSMRNLLGFTSKLSTTLIPHNAQTDPLSGPTPFSSIFMD
TCRGLGNAKLSLNGVDIPANAQKLLRDALGLKDTHSSPTR
NVIDHGISRHDAEQIARESSGSDKQKAEVVEFLCHPEAAT
AICSAFYQSFNVPALTLTHERISKASEYNAERSTPNACIN
ISISQSSDGNIYVTSHTGVLIMAPEDRPNEMGMLTNRTSY
EVPQGVKCIIDEMVSALQPRYAASETYLQN
|
| B: |
KSWDEMSCAEKLFKVLSFGLWNPTYSRSERQSFQELLTVL
EPVYPLPNELGRVSARFSDGSSLRISVTNSELVEAEIRTA
NNEKITVLLESNEQNRLLQSLPIDRHMPYIQVHRALSEMD
LTDTTSMRNLLGFTSKLSTTLIPHNAQTDPLSGPTPFSSI
FMDTCRGLGNAKLSLNGVDIPANAQKLLRDALGLKDTHSS
PTRNVIDHGISRHDAEQIARESSGSDKQKAEVVEFLCHPE
AATAICSAFYQSFNVPALTLTHERISKASEYNAERSLDTP
NACINISISQSSDGNIYVTSHTGVLIMAPEDRPNEMGMLT
NRTSYEVPQGVKCIIDEMVSALQPRYAASETYLQN
|
| C: |
KKSWDEMSCAEKLFKVLSFGLWNPTYSRSERQSFQELLTV
LEPVYPLPNELGRVSARFSDGSSLRISVTNSELVEAEIRT
ANNEKITVLLESNEQNRLLQSLPIDRHMPYIQVHRALLTD
TTSMRNLLGFTSKLSTTLIPHNAQTDPLSGPTPFSSIFMD
TCRGLGNAKLSLNGVDIPANAQKLLRDALGLKDTHSSPTR
NVIDHGISRHDAEQIARESSGSDKQKAEVVEFLCHPEAAT
AICSAFYQSFNVPALTLTHERISKASEYNAEPNACINISI
SQSSDGNIYVTSHTGVLIMAPEDRPNEMGMLTNRTSYEVP
QGVKCIIDEMVSALQPRYAASETYL
|
| D: |
KKSWDEMSCAEKLFKVLSFGLWNPTYSRSERQSFQELLTV
LEPVYPLPNELGRVSARFSDGSSLRISVTNSELVEAEIRT
ANNEKITVLLESNEQNRLLQSLPIDRHMPYIQVHRALLTD
TTSMRNLLGFTSKLSTTLIPHNAQTDPLSGPTPFSSIFMD
TCRGLGNAKLSLNGVDIPANAQKLLRDALGLKDTHSSPTR
NVIDHGISRHDAEQIARESSGSDKQKAEVVEFLCHPEAAT
AICSAFYQSFNVPALTLTHERISKASEYNAERDTPNACIN
ISISQSSDGNIYVTSHTGVLIMAPEDRPNEMGMLTNRTSY
EVPQGVKCIIDEMVSALQPRYAASETYL
|
| E: |
AVLDVLKFYDSNTV
|
| F: |
AVLDVLKFYDSN
|
| G: |
VLDVLKFYDS
|
| H: |
AVLDVLKFYDSNT
|
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Description
|
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Functional site
|
|
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1)
|
chain |
F |
| residue |
128 |
| type |
MOD_RES |
| sequence |
K
|
| description |
N6-acetyllysine => ECO:0007744|PubMed:19608861
|
| source |
Swiss-Prot : SWS_FT_FI1
|
|
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2)
|
chain |
G |
| residue |
128 |
| type |
MOD_RES |
| sequence |
K
|
| description |
N6-acetyllysine => ECO:0007744|PubMed:19608861
|
| source |
Swiss-Prot : SWS_FT_FI1
|
|
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3)
|
chain |
H |
| residue |
128 |
| type |
MOD_RES |
| sequence |
K
|
| description |
N6-acetyllysine => ECO:0007744|PubMed:19608861
|
| source |
Swiss-Prot : SWS_FT_FI1
|
|
|
4)
|
chain |
E |
| residue |
128 |
| type |
MOD_RES |
| sequence |
K
|
| description |
N6-acetyllysine => ECO:0007744|PubMed:19608861
|
| source |
Swiss-Prot : SWS_FT_FI1
|
|
|
5)
|
chain |
H |
| residue |
134 |
| type |
MOD_RES |
| sequence |
T
|
| description |
Phosphothreonine => ECO:0007744|PubMed:23186163
|
| source |
Swiss-Prot : SWS_FT_FI2
|
|
|
6)
|
chain |
E |
| residue |
134 |
| type |
MOD_RES |
| sequence |
T
|
| description |
Phosphothreonine => ECO:0007744|PubMed:23186163
|
| source |
Swiss-Prot : SWS_FT_FI2
|
|
|
|