Structure of PDB 5l6v Chain K

Receptor sequence

>5l6vK (length=421) Species: 83333 (Escherichia coli K-12)

LMLARQLPLKSVALILAGGRGTRLKDLTNKRAKPAVHFGGKFRIIDFALS
NCINSGIRRMGVITQYQSHTLVQHIQRGWSFFNEEMNEFVDLLPAQQRMK
GENWYRGTADAVTQNLDIIRRYKAEYVVILAGDHIYKQDYSRMLIDHVEK
GARCTVACMPVPIEEASAFGVMAVDENDKIIEFVEKPANPPSMPNDPSKS
LASMGIYVFDADYLYELLEEDDRDENSSHDFGKDLIPKITEAGLAYAHPF
PLSCVQSDPDAEPYWRDVGTLEAYWKANLDLASVVPELDMYDRNWPIRTY
NESLPPAKFVQDRSGSHGMTLNSLVSGGCVISGSVVVQSVLFSRVRVNSF
CNIDSAVLLPEVWVGRSCRLRRCVIDRACVIPEGMVIGENAEEDARRFYR
SEEGIVLVTREMLRKLGHKQE

3D structure

• PDB: 5l6v Structural Basis of Glycogen Biosynthesis Regulation in Bacteria.
• Chain: K
• Resolution: 2.667 Å

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	GLC	K	H143 F178 E194 S212	H134 F169 E185 S203
BS02	FRU	K	A140 D142	A131 D133
BS03	AMP	K	R40 H46 R52 T79 E370 R386 A387	R31 H37 R43 T70 E361 R377 A378

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

External links

• PDB: RCSB:5l6v, PDBe:5l6v, PDBj:5l6v
• PDBsum: 5l6v
• PubMed: 27545622
• UniProt: P0A6V1|GLGC_ECOLI Glucose-1-phosphate adenylyltransferase (Gene Name=glgC)