Structure of PDB 6s6x Chain A

Receptor sequence
>6s6xA (length=1472) Species: 192 (Azospirillum brasilense) [Search protein sequence]
CGVGFIAAIDGKPRRSVVEKGIEALKAVWHRGAVDADGKTGDGAGIHVAV
PQKFFKDHVKVIGHRAPDNKLAVGQVFLPRISLDAQEACRCIVETEILAF
GYYIYGWRQVPINVDIIGEKANATRPEIEQIIVGNNKGVSDEQFELDLYI
IRRRIEKAVKGEQINDFYICSLSARSIIYKGMFLAEQLTTFYPDLLDERF
ESDFAIYHQRYSTNTFPTWPLAQPFRMLAHNGEINTVKGNVNWMKAHETR
MEHPAFGTHMQDLKPVIGVGLSDSGSLDTVFEVMVRAGRTAPMVKMMLVP
QALTSSQTTPDNHKALIQYCNSVMEPWDGPAALAMTDGRWVVGGMDRNGL
RPMRYTITTDGLIIGGSETGMVKIDETQVIEKGRLGPGEMIAVDLQSGKL
YRDRELKDHLATLKPWDKWVQNTTHLDELVKTASLKGEPSDMDKAELRRR
QQAFGLTMEDMELILHPMVEDGKEAIGSMGDDSPIAVLSDKYRGLHHFFR
QNFSQVTNPPIDSLRERRVMSLKTRLGNLGNILDEDETQTRLLQLESPVL
TTAEFRAMRDYMGDTAAEIDATFPVDGGPEALRDALRRIRQETEDAVRGG
ATHVILTDEAMGPARAAIPAILATGAVHTHLIRSNLRTFTSLNVRTAEGL
DTHYFAVLIGVGATTVNAYLAQEAIAERHRRGLFGSMPLEKGMANYKKAI
DDGLLKIMSKMGISVISSYRGGGNFEAIGLSRALVAEHFPAMVSRISGIG
LNGIQKKVLEQHATAYNEEVVALPVGGFYRFRKSGDRHGWEGGVIHTLQQ
AVTNDSYTTFKKYSEQVNKRPPMQLRDLLELRSTKAPVPVDEVESITAIR
KRFITPGMSMGALSPEAHGTLNVAMNRIGAKSDSGEGGEDPARFRPDKNG
DNWNSAIKQVASGRFGVTAEYLNQCRELEIKVAQGAKPGEGGQLPGFKVT
EMIARLRHSTPGVMLISPPPHHDIYSIEDLAQLIYDLKQINPDAKVTVKL
VSRSGIGTIAAGVAKANADIILISGNSGGTGASPQTSIKFAGLPWEMGLS
EVHQVLTLNRLRHRVRLRTDGGLKTGRDIVIAAMLGAEEFGIGTASLIAM
GCIMVRQCHSNTCPVGVCVQDDKLRQKFVGTPEKVVNLFTFLAEEVREIL
AGLGFRSLNEVIGRTDLLHQVSRGAEHLDDLDLNPRLAQVDPGENARYCT
LQGRNEVPDTLDARIVADARPLFEEGEKMQLAYNARNTQRAIGTRLSSMV
TRKFGMFGLQPGHITIRLRGTAGQSLGAFAVQGIKLEVMGDANDYVGKGL
SGGTIVVRPTTSSPLETNKNTIIGNTVLYGATAGKLFAAGQAGERFAVRN
SGATVVVEGCGSNGCEYMTGGTAVILGRVGDNFAAGMTGGMAYVYDLDDS
LPLYINDESVIFQRIEVGHYESQLKHLIEEHVTETQSRFAAEILNDWARE
VTKFWQVVPKEMLNRLEVPVHL
3D structure
PDB6s6x Cryo-EM Structures of Azospirillum brasilense Glutamate Synthase in Its Oligomeric Assemblies.
ChainA
Resolution3.5 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 M479 E886 Q934 K937 Q943
Enzyme Commision number 1.4.1.13: glutamate synthase (NADPH).
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 FMN A P856 G857 M858 E886 K999 G1029 T1030 G1071 G1072 I1092 G1093 T1094 P856 G857 M858 E886 K999 G1029 T1030 G1071 G1072 I1092 G1093 T1094
BS02 F3S A C1102 I1103 M1104 V1105 R1106 Q1107 C1108 C1113 C1102 I1103 M1104 V1105 R1106 Q1107 C1108 C1113
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

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:6s6x, PDBe:6s6x, PDBj:6s6x
PDBsum6s6x
PubMed31473159
UniProtQ05755|GLTB_AZOBR Glutamate synthase [NADPH] large chain (Gene Name=gltB)

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