Structure of PDB 1ea0 Chain B

Receptor sequence
>1ea0B (length=1452) Species: 192 (Azospirillum brasilense) [Search protein sequence]
CGVGFIAAIDGKPRRSVVEKGIEALKAVWHRGAVDADGKTGDGAGIHVAV
PQKFFKDHVKVIGHRAPDNKLAVGQVFLPRISLDAQEACRCIVETEILAF
GYYIYGWRQVPINVDIIGEKANATRPEIEQIIVGNNKGVSDEQFELDLYI
IRRRIEKAVKGEQINDFYICSLSARSIIYKGMFLAEQLTTFYPDLLDERF
ESDFAIYHQRYSTNTFPTWPLAQPFRMLAHNGEINTVKGNVNWMKAHETR
MEHPAFGTHMQDLKPVIGVGLSDSGSLDTVFEVMVRAGRTAPMVKMMLVP
QALTTTPDNHKALIQYCNSVMEPWDGPAALAMTDGRWVVGGMDRNGLRPM
RYTITTDGLIIGGSETGMVKIDETQVIEKGRLGPGEMIAVDLQSGKLYRD
RELKDHLATLKPWDKWVQNTTHLDELVKTASLKGEPSDMDKAELRRRQQA
FGLTMEDMELILHPMVEDGKEAIGSMGDDSPIAVLSDKYRGLHHFFRQNF
SQVTNPPIDSLRERRVMSLKTRLGNLGNILDEDETQTRLLQLESPVLTTA
EFRAMRDYMGDTAAEIDATFPVDGGPEALRDALRRIRQETEDAVRGGATH
VILTDEAMGPARAAIPAILATGAVHTHLIRSNLRTFTSLNVRTAEGLDTH
YFAVLIGVGATTVNAYLAQEAIAERHRRGLFGSMPLEKGMANYKKAIDDG
LLKIMSKMGISVISSYRGGGNFEAIGLSRALVAEHFPAMVSRISGIGLNG
IQKKVLEQHATAYNEEVVALPVGGFYRFRKSGDRHGWEGGVIHTLQQAVT
NDSYTTFKKYSEQVNKRPPMQLRDLLELRSTKAPVPVDEVESITAIRKRF
ITPGMSMGALSPEAHGTLNVAMNRIGAKSDSGEGGEDPARFRPDKNGDNW
NSAIKQVASGRFGVTAEYLNQCRELEIKVAQGAKPGEGGQLPGFKVTEMI
ARLRHSTPGVMLISPPPHHDIYSIEDLAQLIYDLKQINPDAKVTVKLVSR
SGIGTIAAGVAKANADIILISGNSGGTGASPQTSIKFAGLPWEMGLSEVH
QVLTLNRLRHRVRLRTDGGLKTGRDIVIAAMLGAEEFGIGTASLIAMGCI
MVRQCHSNTCPVGVCVQDDKLRQKFVGTPEKVVNLFTFLAEEVREILAGL
GFRSLNEVIGRTDLLHQVDLDLNPRLAQVDPGGRNEVPDTLDARIVADAR
PLFEEGEKMQLAYNARNTQRAIGTRLSSMVTRKFGMFGLQPGHITIRLRG
TAGQSLGAFAVQGIKLEVMGDANDYVGKGLSGGTIVVRPTTSSPLETNKN
TIIGNTVLYGATAGKLFAAGQAGERFAVRNSGATVVVEGCGSNGCEYMTG
GTAVILGRVGDNFAAGMTGGMAYVYDLDDSLPLYINDESVIFQRIEVGHY
ESQLKHLIEEHVTETQSRFAAEILNDWAREVTKFWQVVPKEMLNRLEVPV
HL
3D structure
PDB1ea0 Cross-Talk and Ammonia Channeling between Active Centers in the Unexpected Domain Arrangement of Glutamate Synthase
ChainB
Resolution3.0 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 M476 E883 Q931 K934 Q940
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

View graph for
Molecular Function

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Biological Process
External links
PDB RCSB:1ea0, PDBe:1ea0, PDBj:1ea0
PDBsum1ea0
PubMed11188694
UniProtQ05755|GLTB_AZOBR Glutamate synthase [NADPH] large chain (Gene Name=gltB)

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