Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

5B48

2-Oxoacid:Ferredoxin Oxidoreductase 1 from Sulfolobus tokodai

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0006086biological_processacetyl-CoA biosynthetic process from pyruvate
A0006979biological_processresponse to oxidative stress
A0016491molecular_functionoxidoreductase activity
A0016903molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors
A0018491molecular_function2-oxobutyrate synthase activity
A0019164molecular_functionpyruvate synthase activity
A0047553molecular_function2-oxoglutarate synthase activity
B0000287molecular_functionmagnesium ion binding
B0003824molecular_functioncatalytic activity
B0006086biological_processacetyl-CoA biosynthetic process from pyruvate
B0016491molecular_functionoxidoreductase activity
B0018491molecular_function2-oxobutyrate synthase activity
B0019164molecular_functionpyruvate synthase activity
B0030976molecular_functionthiamine pyrophosphate binding
B0046872molecular_functionmetal ion binding
B0047553molecular_function2-oxoglutarate synthase activity
B0051539molecular_function4 iron, 4 sulfur cluster binding
C0003824molecular_functioncatalytic activity
C0006086biological_processacetyl-CoA biosynthetic process from pyruvate
C0006979biological_processresponse to oxidative stress
C0016491molecular_functionoxidoreductase activity
C0016903molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors
C0018491molecular_function2-oxobutyrate synthase activity
C0019164molecular_functionpyruvate synthase activity
C0047553molecular_function2-oxoglutarate synthase activity
D0000287molecular_functionmagnesium ion binding
D0003824molecular_functioncatalytic activity
D0006086biological_processacetyl-CoA biosynthetic process from pyruvate
D0016491molecular_functionoxidoreductase activity
D0018491molecular_function2-oxobutyrate synthase activity
D0019164molecular_functionpyruvate synthase activity
D0030976molecular_functionthiamine pyrophosphate binding
D0046872molecular_functionmetal ion binding
D0047553molecular_function2-oxoglutarate synthase activity
D0051539molecular_function4 iron, 4 sulfur cluster binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue SF4 B 401
ChainResidue
BCYS12
BCYS15
BCYS46
BCYS197
BTHR199

site_idAC2
Number of Residues23
Detailsbinding site for residue TDN B 402
ChainResidue
ALEU322
AARG344
ATHR349
APRO352
BILE44
BGLY45
BCYS46
BSER47
BHIS65
BASP90
BGLY91
BASP92
BASN118
BVAL120
BTYR121
BGLY122
BLEU123
BMG403
CGLU325
ATYR253
APRO254
AGLU294
APRO318

site_idAC3
Number of Residues4
Detailsbinding site for residue MG B 403
ChainResidue
BASP90
BASN118
BVAL120
BTDN402

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues18
DetailsBINDING: BINDING => ECO:0000269|PubMed:27619895, ECO:0007744|PDB:5B48
ChainResidueDetails
BCYS197
DCYS12
DCYS15
DCYS46
DASP90
DGLY91
DASN118
DVAL120
DGLY122
DCYS197
BCYS12
BCYS15
BCYS46
BASP90
BGLY91
BASN118
BVAL120
BGLY122

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q96XT4
ChainResidueDetails
DILE44
DHIS65
BILE44
BHIS65

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Plays an important role in the binding of CoA => ECO:0000269|PubMed:19027887
ChainResidueDetails
DLYS125
BLYS125

220472

PDB entries from 2024-05-29

PDB statisticsPDBj update infoContact PDBjnumon