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1OFD

Glutamate Synthase from Synechocystis sp in complex with 2-Oxoglutarate at 2.0 Angstrom resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0006537biological_processglutamate biosynthetic process
A0006541biological_processglutamine metabolic process
A0015930molecular_functionglutamate synthase activity
A0016040molecular_functionglutamate synthase (NADH) activity
A0016041molecular_functionglutamate synthase (ferredoxin) activity
A0016491molecular_functionoxidoreductase activity
A0016638molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors
A0019676biological_processammonia assimilation cycle
A0046872molecular_functionmetal ion binding
A0051538molecular_function3 iron, 4 sulfur cluster binding
A0097054biological_processL-glutamate biosynthetic process
B0006537biological_processglutamate biosynthetic process
B0006541biological_processglutamine metabolic process
B0015930molecular_functionglutamate synthase activity
B0016040molecular_functionglutamate synthase (NADH) activity
B0016041molecular_functionglutamate synthase (ferredoxin) activity
B0016491molecular_functionoxidoreductase activity
B0016638molecular_functionoxidoreductase activity, acting on the CH-NH2 group of donors
B0019676biological_processammonia assimilation cycle
B0046872molecular_functionmetal ion binding
B0051538molecular_function3 iron, 4 sulfur cluster binding
B0097054biological_processL-glutamate biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues24
DetailsBINDING SITE FOR RESIDUE FMN A 3508
ChainResidue
AGLY874
AGLY1063
AGLY1064
ATHR1065
AGLY1066
AASP1105
AGLY1106
AGLY1107
AGLY1128
ASER1129
AILE1130
AMET875
AMET1132
AHOH2703
AHOH2704
AHOH2705
AAKG3510
ASER876
AGLY902
AGLU903
AGLN944
ALYS966
AGLN969
ALYS1034

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE F3S A 3509
ChainResidue
AMET1132
ACYS1137
AILE1138
AMET1139
AALA1140
AARG1141
AVAL1142
ACYS1143
ACYS1148
AALA1153

site_idAC3
Number of Residues13
DetailsBINDING SITE FOR RESIDUE AKG A 3510
ChainResidue
ASER876
AALA879
AGLU903
AGLN969
ALYS972
AGLY977
AGLN978
AARG992
ATHR1065
AGLY1066
AHOH2463
AHOH2487
AFMN3508

site_idAC4
Number of Residues23
DetailsBINDING SITE FOR RESIDUE FMN B 3508
ChainResidue
BGLY874
BMET875
BSER876
BGLY902
BGLU903
BGLN944
BLYS966
BGLN969
BLYS1034
BGLY1063
BGLY1064
BTHR1065
BGLY1066
BASP1105
BGLY1106
BGLY1107
BGLY1128
BSER1129
BILE1130
BHOH2535
BHOH2716
BHOH2717
BAKG3510

site_idAC5
Number of Residues10
DetailsBINDING SITE FOR RESIDUE F3S B 3509
ChainResidue
BMET1132
BCYS1137
BILE1138
BMET1139
BALA1140
BARG1141
BVAL1142
BCYS1143
BCYS1148
BALA1153

site_idAC6
Number of Residues14
DetailsBINDING SITE FOR RESIDUE AKG B 3510
ChainResidue
BSER876
BALA879
BGLU903
BGLN969
BLYS972
BGLY977
BGLN978
BARG992
BTHR1065
BGLY1066
BALA1067
BHOH2718
BHOH2719
BFMN3508

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: For GATase activity => ECO:0000250
ChainResidueDetails
ACYS1
BCYS1

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ACYS1137
ACYS1143
ACYS1148
BCYS1137
BCYS1143
BCYS1148

Catalytic Information from CSA
site_idCSA1
Number of Residues3
Detailsa catalytic site defined by CSA, PubMed 11967268, 12818206
ChainResidueDetails
ALYS972
AGLU903
ACYS1

site_idCSA2
Number of Residues3
Detailsa catalytic site defined by CSA, PubMed 11967268, 12818206
ChainResidueDetails
BLYS972
BGLU903
BCYS1

site_idMCSA1
Number of Residues9
DetailsM-CSA 111
ChainResidueDetails
ACYS1covalently attached, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AARG31activator, electrostatic stabiliser, hydrogen bond acceptor
APHE207electrostatic stabiliser, hydrogen bond donor
AASN227electrostatic stabiliser, hydrogen bond donor
AGLY228electrostatic stabiliser, hydrogen bond donor
AGLU903electrostatic stabiliser, hydrogen bond acceptor
AGLN969electrostatic stabiliser, hydrogen bond acceptor
ALYS972activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AGLN978activator, hydrogen bond donor

site_idMCSA2
Number of Residues9
DetailsM-CSA 111
ChainResidueDetails
BCYS1covalently attached, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BARG31activator, electrostatic stabiliser, hydrogen bond acceptor
BPHE207electrostatic stabiliser, hydrogen bond donor
BASN227electrostatic stabiliser, hydrogen bond donor
BGLY228electrostatic stabiliser, hydrogen bond donor
BGLU903electrostatic stabiliser, hydrogen bond acceptor
BGLN969electrostatic stabiliser, hydrogen bond acceptor
BLYS972activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BGLN978activator, hydrogen bond donor

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PDB entries from 2024-10-09

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