Structure of PDB 6s6s Chain A

Receptor sequence
>6s6sA (length=1468) Species: 192 (Azospirillum brasilense) [Search protein sequence]
CGVGFIAAIDGKPRRSVVEKGIEALKAVWHRGAVDADGKTGDGAGIHVAV
PQKFFKDHVKVIGHRAPDNKLAVGQVFLPRISLDAQEACRCIVETEILAF
GYYIYGWRQVPINVDIIGEKANATRPEIEQIIVGNNKGVSDEQFELDLYI
IRRRIEKAVKGEQINDFYICSLSARSIIYKGMFLAEQLTTFYPDLLDERF
ESDFAIYHQRYSTNTFPTWPLAQPFRMLAHNGEINTVKGNVNWMKAHETR
MEHPAFGTHMQDLKPVIGVGLSDSGSLDTVFEVMVRAGRTAPMVKMMLVP
QALTSSQTTPDNHKALIQYCNSVMEPWDGPAALAMTDGRWVVGGMDRNGL
RPMRYTITTDGLIIGGSETGMVKIDETQVIEKGRLGPGEMIAVDLQSGKL
YRDRELKDHLATLKPWDKWVQNTTHLDELVKTASLKDMDKAELRRRQQAF
GLTMEDMELILHPMVEDGKEAIGSMGDDSPIAVLSDKYRGLHHFFRQNFS
QVTNPPIDSLRERRVMSLKTRLGNLGNILDEDETQTRLLQLESPVLTTAE
FRAMRDYMGDTAAEIDATFPVDGGPEALRDALRRIRQETEDAVRGGATHV
ILTDEAMGPARAAIPAILATGAVHTHLIRSNLRTFTSLNVRTAEGLDTHY
FAVLIGVGATTVNAYLAQEAIAERHRRGLFGSMPLEKGMANYKKAIDDGL
LKIMSKMGISVISSYRGGGNFEAIGLSRALVAEHFPAMVSRISGIGLNGI
QKKVLEQHATAYNEEVVALPVGGFYRFRKSGDRHGWEGGVIHTLQQAVTN
DSYTTFKKYSEQVNKRPPMQLRDLLELRSTKAPVPVDEVESITAIRKRFI
TPGMSMGALSPEAHGTLNVAMNRIGAKSDSGEGGEDPARFRPDKNGDNWN
SAIKQVASGRFGVTAEYLNQCRELEIKVAQGAKPGEGGQLPGFKVTEMIA
RLRHSTPGVMLISPPPHHDIYSIEDLAQLIYDLKQINPDAKVTVKLVSRS
GIGTIAAGVAKANADIILISGNSGGTGASPQTSIKFAGLPWEMGLSEVHQ
VLTLNRLRHRVRLRTDGGLKTGRDIVIAAMLGAEEFGIGTASLIAMGCIM
VRQCHSNTCPVGVCVQDDKLRQKFVGTPEKVVNLFTFLAEEVREILAGLG
FRSLNEVIGRTDLLHQVSRGAEHLDDLDLNPRLAQVDPGENARYCTLQGR
NEVPDTLDARIVADARPLFEEGEKMQLAYNARNTQRAIGTRLSSMVTRKF
GMFGLQPGHITIRLRGTAGQSLGAFAVQGIKLEVMGDANDYVGKGLSGGT
IVVRPTTSSPLETNKNTIIGNTVLYGATAGKLFAAGQAGERFAVRNSGAT
VVVEGCGSNGCEYMTGGTAVILGRVGDNFAAGMTGGMAYVYDLDDSLPLY
INDESVIFQRIEVGHYESQLKHLIEEHVTETQSRFAAEILNDWAREVTKF
WQVVPKEMLNRLEVPVHL
3D structure
PDB6s6s Cryo-EM Structures of Azospirillum brasilense Glutamate Synthase in Its Oligomeric Assemblies.
ChainA
Resolution3.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C1 R31 Y211 N231 G232 M479 E886 Q934 K937 Q943
Catalytic site (residue number reindexed from 1) C1 R31 Y211 N231 G232 M475 E882 Q930 K933 Q939
Enzyme Commision number 1.4.1.13: glutamate synthase (NADPH).
Interaction with ligand
Gene Ontology
Molecular Function
GO:0004355 glutamate synthase (NADPH) activity
GO:0015930 glutamate synthase activity
GO:0016491 oxidoreductase activity
GO:0016638 oxidoreductase activity, acting on the CH-NH2 group of donors
GO:0046872 metal ion binding
GO:0051538 3 iron, 4 sulfur cluster binding
Biological Process
GO:0006537 glutamate biosynthetic process
GO:0006541 glutamine metabolic process
GO:0019676 ammonia assimilation cycle
GO:0097054 L-glutamate biosynthetic process

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Molecular Function

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Biological Process
External links
PDB RCSB:6s6s, PDBe:6s6s, PDBj:6s6s
PDBsum6s6s
PubMed31473159
UniProtQ05755|GLTB_AZOBR Glutamate synthase [NADPH] large chain (Gene Name=gltB)

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