Structure of PDB 2uu7 Chain N

Receptor sequence
>2uu7N (length=370) Species: 9615 (Canis lupus familiaris) [Search protein sequence]
TSASSHLNKGIKQVYMSLPQGEKVQAMYIWIDGTGEGLRCKTRTLDSEPK
GVEELPEWNFDGSSTFQSEGSNSDMYLVPAAMFRDPFRKDPNKLVFCEVF
KYNRKPAETNLRHTCKRIMDMVSNQHPWFGMEQEYTLMGTDGHPFGWPSN
GFPGPQGPYYCGVGADKAYGRDIVEAHYRACLYAGIKIAGTNAEVMPAQW
EFQIGPCEGIDMGDHLWVARFILHRVCEDFGVIATFDPKPIPGNWNGAGC
HTNFSTKAMREENGLKYIEESIEKLSKRHQYHIRAYDPKGGLDNARRLTG
FHETSNINDFSAGVANRGASIRIPRTVGQEKKGYFEDRRPSANCDPFSVT
EALIRTCLLNETGDEPFQYK
3D structure
PDB2uu7 Crystal Structures of Mammalian Glutamine Synthetases Illustrate Substrate-Induced Conformational Changes and Provide Opportunities for Drug and Herbicide Design.
ChainN
Resolution3.0 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 MG N E136 E196 E203 E134 E194 E201
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004356 glutamine synthetase activity
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:2uu7, PDBe:2uu7, PDBj:2uu7
PDBsum2uu7
PubMed18005987
UniProtQ8HZM5|GLNA_CANLF Glutamine synthetase (Gene Name=GLUL)

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