Structure of PDB 1ofd Chain A

Receptor sequence

>1ofdA (length=1491) Species: 1148 (Synechocystis sp. PCC 6803)

CGVGFIANLRGKPDHTLVEQALKALGCMEHRGGCSADNDSGDGAGVMTAI
PRELLAQWFNTRNLPMPDGDRLGVGMVFLPQEPSAREVARAYVEEVVRLE
KLTVLGWREVPVNSDVLGIQAKNNQPHIEQILVTCPEGCAGDELDRRLYI
ARSIIGKKLAEDFYVCSFSCRTIVYKGMVRSIILGEFYLDLKNPGYTSNF
AVYHRRFSTNTMPKWPLAQPMRLLGHNGEINTLLGNINWMAAREKELEVS
GWTKAELEALTPIVNQANSDSYNLDSALELLVRTGRSPLEAAMILVPEAY
KNQPALKDYPEISDFHDYYSGLQEPWDGPALLVFSDGKIVGAGLDRNGLR
PARYCITKDDYIVLGSEAGVVDLPEVDIVEKGRLAPGQMIAVDLAEQKIL
KNYQIKQQAAQKYPYGEWIKIQRQTVASDSFAEKTLFNDAQTVLQQQAAF
GYTAEDVEMVVVPMASQGKEPTFCMGDDTPLAVLSHKPRLLYDYFKQRFA
QVTNPPIDPLRENLVMSLAMFLGKRGNLLEPKAESARTIKLRSPLVNEVE
LQAIKTGQLQVAEVSTLYDLDGVNSLEDALTNLVKTAIATVQAGAEILVL
TDRPNGAILTENQSFIPPLLAVGAVHHHLIRAGLRLKASLIVDTAQCWST
HHFACLVGYGASAICPYLALESVRQWWLDEKTQKLMENGRLDRIDLPTAL
KNYRQSVEAGLFKILSKMGISLLASYHGAQIFEAIGLGAELVEYAFAGTT
SRVGGLTIADVAGEVMVFHGMAFKKLENFGFVNYRPGGEYHMNSPEMSKS
LHKAVAAYDHYELYRQYLKDRPVTALRDLLDFNADQPAISLEEVESVESI
VKRFCTGGMSLGALSREAHETLAIAMNRLGAKSNSGEGGEDVVRYLTLDD
VDSEGNSPTLPHLHGLQNGDTANSAIKQIASGRFGVTPEYLMSGKQLEIK
MAQGAKPGEGGQLPGKKVSEYIAMLRRSKPGVTLISPPPHHDIYSIEDLA
QLIYDLHQINPEAQVSVKLVAEIGIGTIAAGVAKANADIIQISGHDGGTG
ASPLSSIKHAGSPWELGVTEVHRVLMENQLRDRVLLRADGGLKTGWDVVM
AALMGAEEYGFGSIAMIAEGCIMARVCHTNNCPVGVATQQERLRQRFKGV
PGQVVNFFYFIAEEVRSLLAHLGYRSLDDIIGRTDLLKVRSDVQLSKTQN
LTLDCLLNLPDTKQNRQWLNHEPVHSNGPVLDDDILADPDIQEAINHQTT
ATKTYRLVNTDRTVGTRLSGAIAKKYGNNGFEGNITLNFQGAAGQSFGAF
NLDGMTLHLQGEANDYVGKGMNGGEIVIVPHPQASFAPEDNVIIGNTCLY
GATGGNLYANGRAGERFAVRNSVGKAVIEGAGDHCCEYMTGGVIVVLGPV
GRNVGAGMTGGLAYFLDEVGDLPEKINPEIITLQRITASKGEEQLKSLIT
AHVEHTGSPKGKAILANWSDYLGKFWQAVPPSEKDSPEANN

3D structure

• PDB: 1ofd The Active Conformation of Glutamate Synthase and its Binding to Ferredoxin
• Chain: A
• Resolution: 2.0 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 M475 E887 Q953 K956 Q962
• 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 E903 Q944 K966 Q969 K1034 G1063 G1064 T1065 G1066 D1105 G1107 G1128 S1129 I1130	G858 M859 S860 E887 Q928 K950 Q953 K1018 G1047 G1048 T1049 G1050 D1089 G1091 G1112 S1113 I1114
BS02	F3S	A	C1137 I1138 M1139 A1140 R1141 V1142 C1143 C1148 V1152 A1153	C1121 I1122 M1123 A1124 R1125 V1126 C1127 C1132 V1136 A1137
BS03	AKG	A	S876 E903 Q969 K972 G977 Q978 R992 T1065 G1066	S860 E887 Q953 K956 G961 Q962 R976 T1049 G1050

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:1ofd, PDBe:1ofd, PDBj:1ofd
• PDBsum: 1ofd
• PubMed: 12818206
• UniProt: P55038|GLTS_SYNY3 Ferredoxin-dependent glutamate synthase 2 (Gene Name=gltS)