Structure of PDB 6shq Chain D

Receptor sequence
>6shqD (length=424) Species: 562 (Escherichia coli) [Search protein sequence]
DHLMLARQLPLKSVALILAGGRGTRLKDLTNKRAKPAVHFGGKFRIIDFA
LSNCINSGIRRMGVITQYQSHTLVQHIQRGWSFFNEEMNEFVDLLPAQQR
MKGENWYRGTADAVTQNLDIIRRYKAEYVVILAGDHIYKQDYSRMLIDHV
EKGARCTVACMPVPIEEASAFGVMAVDENDKIIEFVEKPANPPSMPNDPS
KSLASMGIYVFDADYLYELLEEDDRDENSSHDFGKDLIPKITEAGLAYAH
PFPLSCVQSDPDAEPYWRDVGTLEAYWKANLDLASVVPELDMYDRNWPIR
TYNESLPPAKFVQDRSGSHGMTLNSLVSGGCVISGSVVVQSVLFSRVRVN
SFCNIDSAVLLPEVWVGRSCRLRRCVIDRACVIPEGMVIGENAEEDARRF
YRSEEGIVLVTREMLRKLGHKQER
3D structure
PDB6shq The allosteric control mechanism of bacterial glycogen biosynthesis disclosed by cryoEM.
ChainD
Resolution3.2 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 D R40 H46 R52 T79 E370 R386 A387 R419 R33 H39 R45 T72 E363 R379 A380 R412
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:6shq, PDBe:6shq, PDBj:6shq
PDBsum6shq
PubMed34235472
UniProtP0A6V1|GLGC_ECOLI Glucose-1-phosphate adenylyltransferase (Gene Name=glgC)

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