Structure of PDB 8ecy Chain F

Receptor sequence
>8ecyF (length=371) Species: 9913 (Bos taurus) [Search protein sequence]
ATSASSHLNKGIKQVYMALPQGDKVQAMYIWIDGTGEGLRCKTRTLDSEP
KCIEELPEWNFDGSSTFQSEGSNSDMYLVPAAMFRDPFRKDPNKLVFCEV
FKYNRKPAETNLRHTCKRIMDMVSNQRPWFGMEQEYTLMGTDGHPFGWPS
NGFPGPQGPYYCGVGADKAYGRDIVEAHYRACLYAGIKIGGTNAEVMPAQ
WEFQIGPCEGIDMGDHLWVARFILHRVCEDFGVIATFDPKPIPGNWNGAG
CHTNFSTKAMREENGLKYIEEAIEKLSKRHQYHIRAYDPKGGLDNARRLT
GFHETSNINDFSAGVANRGASIRIPRTVGQEKKGYFEDRRPSANCDPFAV
TEALIRTCLLNETGDEPFQYK
3D structure
PDB8ecy Bestrophin-2 and glutamine synthetase form a complex for glutamate release.
ChainF
Resolution2.0 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.3.1.225: protein S-acyltransferase.
6.3.1.2: glutamine synthetase.
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 MN F E136 E196 E203 E135 E195 E202
BS02 MN F E134 E338 E133 E337
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004356 glutamine synthetase activity
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0016740 transferase activity
GO:0016874 ligase activity
GO:0019706 protein-cysteine S-palmitoyltransferase activity
GO:0046872 metal ion binding
Biological Process
GO:0001525 angiogenesis
GO:0006542 glutamine biosynthetic process
GO:0010594 regulation of endothelial cell migration
GO:0018345 protein palmitoylation
GO:1903670 regulation of sprouting angiogenesis
Cellular Component
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005783 endoplasmic reticulum
GO:0005829 cytosol
GO:0005886 plasma membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:8ecy, PDBe:8ecy, PDBj:8ecy
PDBsum8ecy
PubMed36289327
UniProtP15103|GLNA_BOVIN Glutamine synthetase (Gene Name=GLUL)

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