Structure of PDB 4lni Chain J

Receptor sequence
>4lniJ (length=441) Species: 1423 (Bacillus subtilis) [Search protein sequence]
YTREDIEKLVKEENVKYIRLQFTDILGTIKNVEIPVSQLGKALDNKVMFD
GSSIEGFVRIEESDMYLYPDLNTFVIFPWTAEKGKVARFICDIYNPDGTP
FEGDPRNNLKRILKEMEDLGFSDFNLGPEPEFFLFKLDEKGEPTLELNDK
GGYFDLAPTDLGENCRRDIVLELEEMGFEIEASHHEVAPGQHEIDFKYAG
AVRSCDDIQTFKLVVKTIARKHGLHATFMPKPLFGVNGSGMHCNLSLFKN
GVNAFFDENADLQLSETAKHFIAGIVKHATSFTAVTNPTVNSYKRLVPGY
EAPCYVAWSAQNRSPLIRIPASRGISTRVEVRSVDPAANPYLALSVLLAA
GLDGIKNKLEAPAPIDRNIYVMSKEERMENGIVDLPATLAEALEEFKSNE
VMVKALGEHLFEHFIEAKEIEWDMFRTQVHPWEREQYMSQY
3D structure
PDB4lni Structures of the Bacillus subtilis Glutamine Synthetase Dodecamer Reveal Large Intersubunit Catalytic Conformational Changes Linked to a Unique Feedback Inhibition Mechanism.
ChainJ
Resolution2.5793 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D53 E132 E134 E189 E196 H245 R316 E333 R335
Catalytic site (residue number reindexed from 1) D50 E129 E131 E186 E193 H242 R313 E330 R332
Enzyme Commision number 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 P3S J E134 E189 H245 R298 E304 R316 R335 E131 E186 H242 R295 E301 R313 R332
BS02 ADP J G130 E132 E184 D198 Y201 N247 S249 R321 R331 G127 E129 E181 D195 Y198 N244 S246 R318 R328
BS03 MG J E134 E189 E196 E131 E186 E193
BS04 MG J E132 H245 E333 E129 H242 E330
BS05 MG J E132 E196 E129 E193
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0003824 catalytic activity
GO:0004356 glutamine synthetase activity
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0016595 glutamate binding
GO:0016874 ligase activity
GO:0046872 metal ion binding
GO:0070406 glutamine binding
GO:0140297 DNA-binding transcription factor binding
Biological Process
GO:0006542 glutamine biosynthetic process
GO:0043562 cellular response to nitrogen levels
GO:0045892 negative regulation of DNA-templated transcription
GO:0090295 nitrogen catabolite repression of transcription
GO:1904797 negative regulation of core promoter binding
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4lni, PDBe:4lni, PDBj:4lni
PDBsum4lni
PubMed24158439
UniProtP12425|GLN1A_BACSU Glutamine synthetase (Gene Name=glnA)

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