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3AET

Structure of the light-independent protochlorophyllide reductase catalyzing a key reduction for greening in the dark

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0015979biological_processphotosynthesis
A0015995biological_processchlorophyll biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0016636molecular_functionoxidoreductase activity, acting on the CH-CH group of donors, iron-sulfur protein as acceptor
A0016730molecular_functionoxidoreductase activity, acting on iron-sulfur proteins as donors
A0019685biological_processphotosynthesis, dark reaction
A0030494biological_processbacteriochlorophyll biosynthetic process
A0036070biological_processlight-independent bacteriochlorophyll biosynthetic process
A0046872molecular_functionmetal ion binding
A0051539molecular_function4 iron, 4 sulfur cluster binding
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0015979biological_processphotosynthesis
B0015995biological_processchlorophyll biosynthetic process
B0016163molecular_functionnitrogenase activity
B0016491molecular_functionoxidoreductase activity
B0016636molecular_functionoxidoreductase activity, acting on the CH-CH group of donors, iron-sulfur protein as acceptor
B0016730molecular_functionoxidoreductase activity, acting on iron-sulfur proteins as donors
B0019685biological_processphotosynthesis, dark reaction
B0030494biological_processbacteriochlorophyll biosynthetic process
B0036070biological_processlight-independent bacteriochlorophyll biosynthetic process
B0046148biological_processpigment biosynthetic process
B0046872molecular_functionmetal ion binding
B0051539molecular_function4 iron, 4 sulfur cluster binding
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0015979biological_processphotosynthesis
C0015995biological_processchlorophyll biosynthetic process
C0016491molecular_functionoxidoreductase activity
C0016636molecular_functionoxidoreductase activity, acting on the CH-CH group of donors, iron-sulfur protein as acceptor
C0016730molecular_functionoxidoreductase activity, acting on iron-sulfur proteins as donors
C0019685biological_processphotosynthesis, dark reaction
C0030494biological_processbacteriochlorophyll biosynthetic process
C0036070biological_processlight-independent bacteriochlorophyll biosynthetic process
C0046872molecular_functionmetal ion binding
C0051539molecular_function4 iron, 4 sulfur cluster binding
D0005515molecular_functionprotein binding
D0005524molecular_functionATP binding
D0015979biological_processphotosynthesis
D0015995biological_processchlorophyll biosynthetic process
D0016163molecular_functionnitrogenase activity
D0016491molecular_functionoxidoreductase activity
D0016636molecular_functionoxidoreductase activity, acting on the CH-CH group of donors, iron-sulfur protein as acceptor
D0016730molecular_functionoxidoreductase activity, acting on iron-sulfur proteins as donors
D0019685biological_processphotosynthesis, dark reaction
D0030494biological_processbacteriochlorophyll biosynthetic process
D0036070biological_processlight-independent bacteriochlorophyll biosynthetic process
D0046148biological_processpigment biosynthetic process
D0046872molecular_functionmetal ion binding
D0051539molecular_function4 iron, 4 sulfur cluster binding
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SF4 A 425
ChainResidue
ACYS26
BTHR96
ALEU28
ACYS51
ASER111
ACYS112
AGLY145
BPRO33
BGLY35
BCYS36

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SF4 C 425
ChainResidue
CCYS26
CLEU28
CCYS51
CCYS112
CPRO113
CGLY145
DGLY35
DCYS36
DTHR96

Functional Information from PROSITE/UniProt
site_idPS00699
Number of Residues8
DetailsNITROGENASE_1_1 Nitrogenases component 1 alpha and beta subunits signature 1. VLHGPQGC
ChainResidueDetails
BVAL29-CYS36

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_00353, ECO:0000269|PubMed:20400946
ChainResidueDetails
BASP274
DASP274
ACYS112
CCYS26
CCYS51
CCYS112

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:20400946
ChainResidueDetails
BCYS36
BGLY409
DCYS36
DGLY409

223790

PDB entries from 2024-08-14

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