Structure of PDB 5l6v Chain B

Receptor sequence
>5l6vB (length=421) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
HLMLARQLPLKSVALILAGGRGTRLKDLTNKRAKPAVHFGGKFRIIDFAL
SNCINSGIRRMGVITQYQSHTLVQHIQRGWSFFNEEMNEFVDLLPAQQRM
KGENWYRGTADAVTQNLDIIRRYKAEYVVILAGDHIYKQDYSRMLIDHVE
KGARCTVACMPVPIEEASAFGVMAVDENDKIIEFVEKPANPPSMPNDPSK
SLASMGIYVFDADYLYELLEEDDRDENSSHDFGKDLIPKITEAGLAYAHP
FPLSCVQSDPDAEPYWRDVGTLEAYWKANLDLASVVPELDMYDRNWPIRT
YNESLPPAKFVQDRSGSHGMTLNSLVSGGCVISGSVVVQSVLFSRVRVNS
FCNIDSAVLLPEVWVGRSCRLRRCVIDRACVIPEGMVIGENAEEDARRFY
RSEEGIVLVTREMLRKLGHKQ
3D structure
PDB5l6v Structural Basis of Glycogen Biosynthesis Regulation in Bacteria.
ChainB
Resolution2.667 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.7.7.27: glucose-1-phosphate adenylyltransferase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 AMP B K39 R40 H46 R52 T79 E370 R386 A387 R419 K31 R32 H38 R44 T71 E362 R378 A379 R411
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0005524 ATP binding
GO:0008878 glucose-1-phosphate adenylyltransferase activity
GO:0016208 AMP binding
GO:0016779 nucleotidyltransferase activity
GO:0042802 identical protein binding
Biological Process
GO:0005978 glycogen biosynthetic process
GO:0009058 biosynthetic process
GO:0051289 protein homotetramerization
Cellular Component
GO:0010170 glucose-1-phosphate adenylyltransferase complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5l6v, PDBe:5l6v, PDBj:5l6v
PDBsum5l6v
PubMed27545622
UniProtP0A6V1|GLGC_ECOLI Glucose-1-phosphate adenylyltransferase (Gene Name=glgC)

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