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1DJ7

CRYSTAL STRUCTURE OF 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 Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 201
ChainResidue
AARG80
BLYS62
BHIS64
BHOH204
BHOH216
BHOH236

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SF4 A 120
ChainResidue
AMET79
ACYS85
AHIS86
ACYS87
ACYS55
ACYS74
ACYS76

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

Catalytic Information from CSA
site_idMCSA1
Number of Residues7
DetailsM-CSA 980
ChainResidueDetails
ACYS55electrofuge, electrophile, hydrogen bond acceptor, metal ligand
ACYS57electrofuge, electrophile, metal ligand, nucleofuge, nucleophile, proton acceptor, proton donor
ACYS74metal ligand
ACYS76metal ligand
ACYS85metal ligand
AHIS86electrostatic stabiliser, proton donor
ACYS87activator, covalent catalysis, electrofuge, electrophile, hydrogen bond donor, metal ligand, nucleofuge, nucleophile, proton acceptor, proton donor

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PDB entries from 2024-11-06

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