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6UYK

Dark-operative protochlorophyllide oxidoreductase in the nucleotide-free form.

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide 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
A0051536molecular_functioniron-sulfur cluster binding
A0051539molecular_function4 iron, 4 sulfur cluster binding
B0000166molecular_functionnucleotide binding
B0005524molecular_functionATP binding
B0015979biological_processphotosynthesis
B0015995biological_processchlorophyll biosynthetic process
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
B0046872molecular_functionmetal ion binding
B0051536molecular_functioniron-sulfur cluster binding
B0051539molecular_function4 iron, 4 sulfur cluster binding
C0000166molecular_functionnucleotide 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
C0051536molecular_functioniron-sulfur cluster binding
C0051539molecular_function4 iron, 4 sulfur cluster binding
D0000166molecular_functionnucleotide binding
D0005524molecular_functionATP binding
D0015979biological_processphotosynthesis
D0015995biological_processchlorophyll biosynthetic process
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
D0046872molecular_functionmetal ion binding
D0051536molecular_functioniron-sulfur cluster binding
D0051539molecular_function4 iron, 4 sulfur cluster binding
Functional Information from PDB Data
site_idAC1
Number of Residues10
Detailsbinding site for residue SF4 A 301
ChainResidue
ACYS126
BPHE163
AGLY127
ACYS160
AGLY162
APHE163
BCYS126
BGLY127
BCYS160
BGLY162

site_idAC2
Number of Residues11
Detailsbinding site for residue SF4 C 301
ChainResidue
CVAL20
CCYS126
CGLY127
CCYS160
CGLY162
CPHE163
DCYS126
DGLY127
DCYS160
DGLY162
DPHE163

Functional Information from PROSITE/UniProt
site_idPS00692
Number of Residues14
DetailsNIFH_FRXC_2 NifH/frxC family signature 2. DvLGDVVCGGFAaP
ChainResidueDetails
AASP153-PRO166

site_idPS00746
Number of Residues13
DetailsNIFH_FRXC_1 NifH/frxC family signature 1. EaGGPpaGtGCGG
ChainResidueDetails
AGLU116-GLY128

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues42
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"19006326","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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