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UniProt C1DGZ6

Nitrogenase iron protein gamma chain (C1DGZ6)

Nitrogenase iron protein gamma chain (UniProt C1DGZ6), EC 1.18.6.1: 9 experimental structures on GenesisL1, 5 ligands bound, 23 pockets. Binding sites, pockets, druggability and 3D structures in GL1X.

UniProt
C1DGZ6
Protein
Nitrogenase iron protein gamma chain
EC
1.18.6.1
Experimental structures
9
Predicted models
0
Ligands
5
Pockets
23 · 4 records with a druggable one

Structures

9 records of C1DGZ6 in the MolNFT archive: 9 experimental, 0 predicted.

EntryTitleMethodChainsLigandsPockets
6O0BStructural and Mechanistic Insights into CO2 Activation by Nitrogenase Iron Proteinx-ray diffractionA, BSF4—
6O0BStructural and mechanistic insights into CO2 activation by nitrogenase iron proteinx-ray diffractionA, BSF4—
7UT8CryoEM structure of Azotobacter vinelandii nitrogenase complex (1:1 FeP:MoFeP, ATP-bound) during…electron microscopyE, FSF4, MG, ATP5 (best 0.85)
7UT8Cryoem structure of azotobacter vinelandii nitrogenase complex (1:1 FEP:MOFEP, ATP-bound) during…electron microscopyE, FSF4, MG, ATP—
7UT9CryoEM structure of Azotobacter vinelandii nitrogenase complex (1:1 FeP:MoFeP, ADP/ATP-bound)…electron microscopyE, FMG, ADP, SF4, ATP6 (best 0.84)
7UT9Cryoem structure of azotobacter vinelandii nitrogenase complex (1:1 FEP:MOFEP, ADP/ATP-bound)…electron microscopyE, FMG, ADP, SF4, ATP—
7UTACryoEM structure of Azotobacter vinelandii nitrogenase complex (2:1 FeP:MoFeP) inhibited by BeFx…electron microscopyE, F, G, HSF4, MG, ADP, 0BE10 (best 0.82)
7UTACryoem structure of azotobacter vinelandii nitrogenase complex (2:1 FEP:MOFEP) inhibited by befx…electron microscopyE, F, G, HSF4, MG, ADP, 0BE—
8TC3CryoEM structure of nucleotide-free form of the nitrogenase iron protein from A. vinelandiielectron microscopyA, BSF42 (best 0.79)

Ligands

  • SF4 · Iron/sulfur cluster · in 9 records
  • MG · Magnesium ion · in 6 records
  • ADP · Adenosine-5'-diphosphate · in 4 records
  • ATP · Adenosine-5'-triphosphate · in 4 records
  • 0BE · Beryllium · in 2 records

Elsewhere

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