Structure of PDB 6s6s Chain D

Receptor sequence
>6s6sD (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.
ChainD
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
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 D P856 G857 M858 S859 G1028 G1029 T1030 G1071 G1072 G1093 T1094 P852 G853 M854 S855 G1024 G1025 T1026 G1067 G1068 G1089 T1090
BS02 F3S D C1102 I1103 M1104 V1105 R1106 C1108 C1113 V1117 C1098 I1099 M1100 V1101 R1102 C1104 C1109 V1113
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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