Structure of PDB 1llw Chain A

Receptor sequence

>1llwA (length=1475) Species: 1148 (Synechocystis sp. PCC 6803)

CGVGFIANLRGKPDHTLVEQALKALGCMEHRGGCSADNDSGDGAGVMTAI
PRELLAQWFNTRNLPMPDGDRLGVGMVFLPQEPSAREVARAYVEEVVRLE
KLTVLGWREVPVNSDVLGIQAKNNQPHIEQILVTCPEGCAGDELDRRLYI
ARSIIGKKLAEDFYVCSFSCRTIVYKGMVRSIILGEFYLDLKNPGYTSNF
AVYHRRFSTNTMPKWPLAQPMRLLGHNGEINTLLGNINWMAAREKELEVS
GWTKAELEALTPIVNQANSDSYNLDSALELLVRTGRSPLEAAMILVPEAY
KNQPALKDYPEISDFHDYYSGLQEPWDGPALLVFSDGKIVGAGLDRNGLR
PARYCITKDDYIVLGSEAGVVDLPEVDIVEKGRLAPGQMIAVDLAEQKIL
KNYQIKQQAAQKYPYGEWIKIQDAQTVLQQQAAFGYTAEDVEMVVVPMAS
QGKEPTFCMGDDTPLAVLSHKPRLLYDYFKQRFAQVTNPPIDPLRENLVM
SLAMFLGKRGNLLEPKAEKLRSPLVNEVELQAIKTGQLQVAEVSTLYDLD
GVNSLEDALTNLVKTAIATVQAGAEILVLTDRPNGAILTENQSFIPPLLA
VGAVHHHLIRAGLRLKASLIVDTAQCWSTHHFACLVGYGASAICPYLALE
SVRQWWLDEKTQKLMENGRLDRIDLPTALKNYRQSVEAGLFKILSKMGIS
LLASYHGAQIFEAIGLGAELVEYAFAGTTSRVGGLTIADVAGEVMVFHGM
AFPEMAKKLENFGFVNYRPGGEYHMNSPEMSKSLHKAVAAYYDHYELYRQ
YLKDRPVTALRDLLDFNADQPAISLEEVESVESIVKRFCTGGMSLGALSR
EAHETLAIAMNRLGAKSNSGEGGEDVVRYLTLDDVDSEGNSPTLPHLHGL
QNGDTANSAIKQIASGRFGVTPEYLMSGKQLEIKMAQGAKPGEGGQLPGK
KVSEYIAMLRRSKPGVTLISPPPHHDIYSIEDLAQLIYDLHQINPEAQVS
VKLVAEIGIGTIAAGVAKANADIIQISGHDGGTGASPLSSIKHAGSPWEL
GVTEVHRVLMENQLRDRVLLRADGGLKTGWDVVMAALMGAEEYGFGSIAM
IAEGCIMARVCHTNNCPVGVATQQERLRQRFKGVPGQVVNFFYFIAEEVR
SLLAHLGYRSLDDIIGRTDLLKVRSDVQLSKTQNLTLDCLLNLPDTKQNR
QWLNHEPVHSNGPVLDDDILADPDIQEAINHQTTATKTYRLVNTDRTVGT
RLSGAIAKKYGNNGFEGNITLNFQGAAGQSFGAFNLDGMTLHLQGEANDY
VGKGMNGGEIVIVPHPQASFAPEDNVIIGNTCLYGATGGNLYANGRAGER
FAVRNSVGKAVIEGAGDHCCEYMTGGVIVVLGPVGRNVGAGMTGGLAYFL
DEVGDLPEKINPEIITLQRITASKGEEQLKSLITAHVEHTGSPKGKAILA
NWSDYLGKFWQAVPPSEKDSPEANN

3D structure

• PDB: 1llw Structural studies on the synchronization of catalytic centers in glutamate synthase
• Chain: A
• Resolution: 2.7 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): C1 R31 F207 N227 G228 M475 E903 Q969 K972 Q978
• Catalytic site (residue number reindexed from 1): C1 R31 F207 N227 G228 M459 E871 Q937 K940 Q946
• Enzyme Commision number: 1.4.7.1: glutamate synthase (ferredoxin).

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	G874 M875 S876 G902 E903 Q944 K966 Q969 K1034 G1063 G1064 T1065 G1066 D1105 G1106 G1107 G1128 S1129 M1132	G842 M843 S844 G870 E871 Q912 K934 Q937 K1002 G1031 G1032 T1033 G1034 D1073 G1074 G1075 G1096 S1097 M1100
BS02	F3S	A	C1137 I1138 M1139 A1140 R1141 V1142 C1143 C1148	C1105 I1106 M1107 A1108 R1109 V1110 C1111 C1116
BS03	AKG	A	S876 E903 Q969 K972 G977 Q978 R992 T1065 G1066	S844 E871 Q937 K940 G945 Q946 R960 T1033 G1034

Gene Ontology

Molecular Function

• GO:0015930 glutamate synthase activity
• GO:0016040 glutamate synthase (NADH) activity
• GO:0016041 glutamate synthase (ferredoxin) 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

External links

• PDB: RCSB:1llw, PDBe:1llw, PDBj:1llw
• PDBsum: 1llw
• PubMed: 11967268
• UniProt: P55038|GLTS_SYNY3 Ferredoxin-dependent glutamate synthase 2 (Gene Name=gltS)