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2PUO

Crystal srtucture of the NEM modified 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
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 201
ChainResidue
AARG80
AHOH332
AHOH352
BLYS62
BHIS64

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SF4 A 202
ChainResidue
ACYS85
AHIS86
ACYS87
ACYS55
ACYS74
ACYS76
AMET79

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NEQ A 301
ChainResidue
AVAL35
ACYS57
ACYS87
BMET1
BASN2
BVAL38

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:10649999, ECO:0000269|PubMed:14769790, ECO:0000269|PubMed:17611542, ECO:0000269|PubMed:19132843
ChainResidueDetails
ACYS57

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:10649999, ECO:0000269|PubMed:17611542
ChainResidueDetails
ACYS55
ACYS74
ACYS76
ACYS85

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: Increases the nucleophilicity of the active site Cys => ECO:0000269|PubMed:19132843
ChainResidueDetails
AHIS86

219140

PDB entries from 2024-05-01

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