Structure of PDB 3o6x Chain D

Receptor sequence
>3o6xD (length=638) Species: 272559 (Bacteroides fragilis NCTC 9343) [Search protein sequence]
KMRFFALQELSNRKPLEITTPSNKLSDYYASHVFDRKKMQEYLPKEAYKA
VVDATEKGTPISREMADLIANGMKSWAKSLNVTHYTHWFQPLTKHDGFIE
FGEDGEVIERFSGKLLTAWDGSSPAFVVDTTLCIPTIFIEALDYKTPLLK
ALAAVDKAATEVCQLFDKNITRVFTNLGWEQEYFLVDTSLYNARPDLRLT
GRTLMGHSIPPRVTAFMKELEIECHKLGIPVKTRHNEVAPNQFELAPIFE
NCNLANDHNQLVMDLMKRIARKHHFAVLFHEKPYNGVNGSGKHNNWSLCT
DTGINLFAPGKNPKGNMLFLTFLVNVLMMVHKNQDLLRASIMSAGNSHRL
GANEAPPAILSIFLGSQLSATLDEIRNRTSPFAFTGNRFEFRAAGSSANC
AAAMIAINAAMANQLNEFKASVDKDEAIFRILKENIIASELIRFEGDGYS
EEWKQEAARRGLTNICHVPEALMHYMDNQSRAVLIGERIFNETELACRLE
VELEKYTMKVQIESRVLGDLAINHIVPIAVSYQNRLLENLCRMKEIFSEE
EYEVMSADRKELIKEISHRVSAIKVLVRDMTEARKVANHKENFKEKAFAY
EETVRPYLESIRDHIDHLEMEIDDEIWPLPKYRELLFT
3D structure
PDB3o6x Crystal Structure of Type III Glutamine Synthetase: Surprising Reversal of the Inter-Ring Interface.
ChainD
Resolution3.5 Å
3D
structure
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Enzymatic activity
Enzyme Commision number ?
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 D E215 H342 E472 E180 H293 E390
BS02 MG D E217 E286 E293 E182 E237 E244
BS03 P3S D E215 E217 E286 G338 G340 H342 R398 E403 E180 E182 E237 G289 G291 H293 R349 E354
BS04 ADP D E215 E293 F298 N344 S346 R470 E180 E244 F249 N295 S297 R388
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0003824 catalytic activity
GO:0004356 glutamine synthetase activity
GO:0016874 ligase activity
GO:0046872 metal ion binding
Biological Process
GO:0006542 glutamine biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3o6x, PDBe:3o6x, PDBj:3o6x
PDBsum3o6x
PubMed21481771
UniProtQ5LGP1

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