2c4m/2/1:D/1:C |
>2c4m-a2-m1-cD (length=788) [Search sequence] |
QPLPAALVGSHVRAAAGTPADLATDRKFWTGLSRAVQERIADDWERTREAYGAARQQHYF SAEFLMGRALLNNLTNLGLVDEAAAATRELGHELTDILEIENDAALGNGGLGRLAACFLD SAVTQDYPVTGYGLLYRFGLFRQSFNEGFQVEKPDPWREEEYPFTIRRASDQLVVCFDDM KTRAIPYDMPITGYGTHNVGTLRLWKAEPWEEFDYDAFNAQRFTDAIIERERVSDICRVL YPNDTTYEGKKLRVRQQYFFTSASLQAMIQDHLAHHKDLSNFAEFHSVQLNDTHPVLAIP ELMRLLMDEHDMGWEESWAIVSKTFAYTNHTVLTEALEQWDEQIFQQLFWRVWEIIAEID RRFRLERAADGLDEETINRMAPIQHGTVHMAWIACYAAYSINGVAALHTEIIKAETLADW YALWPEKFNNKTNGVTPRRWLRMINPGLSDLLTRLSGSDDWVTDLDELKKLRSYADDKSV LEELRAIKAANKQDFAEWILERQGIEIDPESIFDVQIKRLHEYKRQLMNALYVLDLYFRI KEDGLTDIPARTVIFGAKAAPGYVRAKAIIKLINSIADLVNNDPEVSPLLKVVFVENYNV SPAEHILPASDVSEQISTAGKEASGTSNMKFMMNGALTLGTMDGANVEIVDSVGEENAYI FGARVEELPALRESYKPYELYETVPGLKRALDALDNGTLNDNNSGLFYDLKHSLIHGYGK DASDTYYVLGDFADYRETRDRMAADYASDPLGWARMAWINICESGRFSSDRTIRDYATEI WKLEPTPA |
>2c4m-a2-m1-cC (length=790) [Search sequence] |
QPLPAALVGSHVRAAAGTPADLATDRKFWTGLSRAVQERIADDWERTREAYGAARQQHYF SAEFLMGRALLNNLTNLGLVDEAAAATRELGHELTDILEIENDAALGNGGLGRLAACFLD SAVTQDYPVTGYGLLYRFGLFRQSFNEGFQVEKPDPWREEEYPFTIRRASDQLVVCFDDM KTRAIPYDMPITGYGTHNVGTLRLWKAEPWEEFDYDAFNAQRFTDAIIERERVSDICRVL YPNDTTYEGKKLRVRQQYFFTSASLQAMIQDHLAHHKDLSNFAEFHSVQLNDTHPVLAIP ELMRLLMDEHDMGWEESWAIVSKTFAYTNHTVLTEALEQWDEQIFQQLFWRVWEIIAEID RRFRLERAADGLDEETINRMAPIQHGTVHMAWIACYAAYSINGVAALHTEIIKAETLADW YALWPEKFNNKTNGVTPRRWLRMINPGLSDLLTRLSGSDDWVTDLDELKKLRSYADDKSV LEELRAIKAANKQDFAEWILERQGIEIDPESIFDVQIKRLHEYKRQLMNALYVLDLYFRI KEDGLTDIPARTVIFGAKAAPGYVRAKAIIKLINSIADLVNNDPEVSPLLKVVFVENYNV SPAEHILPASDVSEQISTAGKEASGTSNMKFMMNGALTLGTMDGANVEIVDSVGEENAYI FGARVEELPALRESYKPYELYETVPGLKRALDALDNGTLNDNNSGLFYDLKHSLIHGYGK DASDTYYVLGDFADYRETRDRMAADYASDPLGWARMAWINICESGRFSSDRTIRDYATEI WKLEPTPAVK |
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PDB ID |
2c4m (database links:
RCSB PDB
PDBe
PDBj
PDBsum) |
Title |
Starch phosphorylase: structural studies explain oxyanion-dependent kinetic stability and regulatory control. |
Assembly ID |
2 |
Resolution |
1.9Å |
Method of structure determination |
X-RAY DIFFRACTION |
Number of inter-chain contacts |
171 |
Sequence identity between the two chains |
1.0 |
PubMed citation |
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Chain 1 |
Chain 2 |
Model ID |
1 |
1 |
Chain ID |
D |
C |
UniProt accession |
Q8KQ56 |
Q8KQ56 |
Species |
1721 (Corynebacterium callunae) |
1721 (Corynebacterium callunae) |
Function annotation |
BioLiP:2c4mD |
BioLiP:2c4mC |
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Switch viewer: [NGL] [JSmol]
Dimer structure:
Chain 1 in red;
Chain 2 in blue.
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Full biological assembly
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