Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

2PVO

Crystal srtucture of the ternary complex between thioredoxin f, ferredoxin, and ferredoxin: thioredoxin reductase

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0009055molecular_functionelectron transfer activity
A0015979biological_processphotosynthesis
A0016491molecular_functionoxidoreductase activity
A0016730molecular_functionoxidoreductase activity, acting on iron-sulfur proteins as donors
A0046872molecular_functionmetal ion binding
A0051536molecular_functioniron-sulfur cluster binding
A0051539molecular_function4 iron, 4 sulfur cluster binding
A0103012molecular_functionferredoxin-thioredoxin reductase activity
B0005515molecular_functionprotein binding
B0015979biological_processphotosynthesis
B0016491molecular_functionoxidoreductase activity
C0015035molecular_functionprotein-disulfide reductase activity
D0005515molecular_functionprotein binding
D0009055molecular_functionelectron transfer activity
D0022900biological_processelectron transport chain
D0046872molecular_functionmetal ion binding
D0051536molecular_functioniron-sulfur cluster binding
D0051537molecular_function2 iron, 2 sulfur cluster binding
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 201
ChainResidue
AARG80
BLYS62

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 202
ChainResidue
ALEU50
AGLY51
ASER52
DGLU34
DPRO36
DTYR37

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SF4 A 300
ChainResidue
ACYS74
ACYS76
AMET79
ACYS85
AHIS86
ACYS87
APHE90
ACYS55

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE FES D 400
ChainResidue
DSER38
DCYS39
DARG40
DGLY42
DALA43
DCYS44
DCYS47
DCYS77

Functional Information from PROSITE/UniProt
site_idPS00197
Number of Residues9
Details2FE2S_FER_1 2Fe-2S ferredoxin-type iron-sulfur binding region signature. CRAGACSTC
ChainResidueDetails
DCYS39-CYS47

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"10649999","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14769790","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17611542","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19132843","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10649999","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17611542","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsSite: {"description":"Increases the nucleophilicity of the active site Cys","evidences":[{"source":"PubMed","id":"19132843","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues3
DetailsRegion: {"description":"Interaction with ferredoxin","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsActive site: {"description":"Nucleophile"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsSite: {"description":"Deprotonates C-terminal active site Cys"}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsSite: {"description":"Contributes to redox potential value"}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues90
DetailsDomain: {"description":"2Fe-2S ferredoxin-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00465","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00465","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"7578051","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1cqg
ChainResidueDetails
CCYS46
CSER49

247536

PDB entries from 2026-01-14

PDB statisticsPDBj update infoContact PDBjnumon