Structure of PDB 1ofe Chain B

Receptor sequence

>1ofeB (length=1485) Species: 1148 (Synechocystis sp. PCC 6803)

CGVGFIANLRGKPDHTLVEQALKALGCMEHRGGCSADNDSGDGAGVMTAI
PRELLAQWFNTRNLPMPDGDRLGVGMVFLPQEPSAREVARAYVEEVVRLE
KLTVLGWREVPVNSDVLGIQAKNNQPHIEQILVTCPEGCAGDELDRRLYI
ARSIIGKKLAEDFYVCSFSCRTIVYKGMVRSIILGEFYLDLKNPGYTSNF
AVYHRRFSTNTMPKWPLAQPMRLLGHNGEINTLLGNINWMAAREKELEVS
GWTKAELEALTPIVNQANSDSYNLDSALELLVRTGRSPLEAAMILVPEAY
KNQPALKDYPEISDFHDYYSGLQEPWDGPALLVFSDGKIVGAGLDRNGLR
PARYCITKDDYIVLGSEAGVVDLPEVDIVEKGRLAPGQMIAVDLAEQKIL
KNYQIKQQAAQKYPYGEWIKIQRQTVASDSFAEKTLFNDAQTVLQQQAAF
GYTAEDVEMVVVPMASQGKEPTFCMGDDTPLAVLSHKPRLLYDYFKQRFA
QVTNPPIDPLRENLVMSLAMFLGKRGNLLEPKAESARTIKLRSPLVNEVE
LQAIKTGQLQVAEVSTLYDNSLEDALTNLVKTAIATVQAGAEILVLTDRP
NGAILTENQSFIPPLLAVGAVHHHLIRAGLRLKASLIVDTAQCWSTHHFA
CLVGYGASAICPYLALESVRQWWLDEKTQKLMENGRLIDLPTALKNYRQS
VEAGLFKILSKMGISLLASYHGAQIFEAIGLGAELVEYAFAGTTSRVGGL
TIADVAGEVMVFHGMAFKKLENFGFVNYRPGGEYHMNSPEMSKSLHKAVA
AYDHYELYRQYLKDRPVTALRDLLDFNADQPAISLEEVESVESIVKRFCT
GGMSLGALSREAHETLAIAMNRLGAKSNSGEGGEDVVRYLTLDDVDSEGN
SPTLPHLHGLQNGDTANSAIKQIASGRFGVTPEYLMSGKQLEIKMAQGAK
PGEGGQLPGKKVSEYIAMLRRSKPGVTLISPPPHHDIYSIEDLAQLIYDL
HQINPEAQVSVKLVAEIGIGTIAAGVAKANADIIQISGHDGGTGASPLSS
IKHAGSPWELGVTEVHRVLMENQLRDRVLLRADGGLKTGWDVVMAALMGA
EEYGFGSIAMIAEGCIMARVCHTNNCPVGVATQQERLRQRFKGVPGQVVN
FFYFIAEEVRSLLAHLGYRSLDDIIGRTDLLKVRSDVQLSKTQNLTLDCL
LNLPDTKQNRQWLNHEPVHSNGPVLDDDILADPDIQEAINHQTTATKTYR
LVNTDRTVGTRLSGAIAKKYGNNGFEGNITLNFQGAAGQSFGAFNLDGMT
LHLQGEANDYVGKGMNGGEIVIVPHPQASFAPEDNVIIGNTCLYGATGGN
LYANGRAGERFAVRNSVGKAVIEGAGDHCCEYMTGGVIVVLGPVGRNVGA
GMTGGLAYFLDEVGDLPEKINPEIITLQRITASKGEEQLKSLITAHVEHT
GSPKGKAILANWSDYLGKFWQAVPPSEKDSPEANN

3D structure

• PDB: 1ofe The Active Conformation of Glutamate Synthase and its Binding to Ferredoxin
• Chain: B
• Resolution: 2.45 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 E881 Q947 K950 Q956
• 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	B	G874 M875 S876 E903 Q944 K966 K1034 G1064 T1065 G1066 D1105 G1107 G1128 S1129 M1132	G852 M853 S854 E881 Q922 K944 K1012 G1042 T1043 G1044 D1083 G1085 G1106 S1107 M1110
BS02	F3S	B	C1137 I1138 A1140 R1141 V1142 C1143 C1148 V1152 A1153	C1115 I1116 A1118 R1119 V1120 C1121 C1126 V1130 A1131
BS03	AKG	B	S876 Q969 K972 Q978 R992 T1065 G1066	S854 Q947 K950 Q956 R970 T1043 G1044
BS04	ONL	B	C1 R206 N227 G228 E229 D270	C1 R206 N227 G228 E229 D270

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