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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
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 Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00465, ECO:0000269|PubMed:7578051
ChainResidueDetails
DCYS39
DCYS44
DCYS47
DCYS77

site_idSWS_FT_FI2
Number of Residues1
DetailsSITE: Deprotonates C-terminal active site Cys
ChainResidueDetails
CASP40
ACYS74
ACYS76
ACYS85

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Contributes to redox potential value
ChainResidueDetails
CGLY47
CPRO48

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

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PDB entries from 2024-11-13

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