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8bts

Nitrogenase MoFe protein from A. vinelandii alpha double mutant C45A/L158C

Method: X-RAY DIFFRACTION Dmax: 186.6 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Nitrogenase protein alpha chain

Azotobacter vinelandii DJ

UniProt C1DGZ7

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count Chain A； UniProt 3–492 Chain C； UniProt 3–492 Not recorded Nitrogenase molybdenum-iron protein beta chain × 2 （P07329） HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 2 ICS iron-sulfur-molybdenum cluster with interstitial carbon × 2 GOL GLYCEROL × 10 SO4 SULFATE ION × 5 1CL FE(8)-S(7) CLUSTER, OXIDIZED × 2 FE FE (III) ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 5.5；293.15 K；The purified enzyme in 50 mM Tris/HCl pH 8.0, 300 mM NaCl, 2 mM dithionite was crystallized at 8 mg.ml-1. Crystallization was performed anaerobically in a tent containing 100 % N2 atmosphere. Crystals were obtained by initial screening at 20 degree Celsius on 96-Well MRC 2-drop crystallization plates in polystyrene (SWISSCI) containing 90 ul of crystallization solution in the reservoir. The protein sample (0.5 ul) was mixed with 0.5 ul reservoir solution. The reservoir solution contained 25 % w/v Polyethylene glycol 3,350, 100 mM BIS-TRIS at pH 5.5, and 200 mM Lithium sulfate. The plate was then incubated in a Coy tent (N2/H2, 97:3) at 20 degree Celsius. Crystals appeared after a few weeks and were soaked in the crystallization solution supplemented with 15 % v/v glycerol as a cryo-protectant before being frozen in liquid nitrogen. Resolution 3.03 Å R-free 0.223
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count Chain H； UniProt 3–492 Chain J； UniProt 3–492 Not recorded Nitrogenase molybdenum-iron protein beta chain × 2 （P07329） HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 2 ICS iron-sulfur-molybdenum cluster with interstitial carbon × 2 GOL GLYCEROL × 2 SO4 SULFATE ION × 5 1CL FE(8)-S(7) CLUSTER, OXIDIZED × 2 FE FE (III) ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 5.5；293.15 K；The purified enzyme in 50 mM Tris/HCl pH 8.0, 300 mM NaCl, 2 mM dithionite was crystallized at 8 mg.ml-1. Crystallization was performed anaerobically in a tent containing 100 % N2 atmosphere. Crystals were obtained by initial screening at 20 degree Celsius on 96-Well MRC 2-drop crystallization plates in polystyrene (SWISSCI) containing 90 ul of crystallization solution in the reservoir. The protein sample (0.5 ul) was mixed with 0.5 ul reservoir solution. The reservoir solution contained 25 % w/v Polyethylene glycol 3,350, 100 mM BIS-TRIS at pH 5.5, and 200 mM Lithium sulfate. The plate was then incubated in a Coy tent (N2/H2, 97:3) at 20 degree Celsius. Crystals appeared after a few weeks and were soaked in the crystallization solution supplemented with 15 % v/v glycerol as a cryo-protectant before being frozen in liquid nitrogen. Resolution 3.03 Å R-free 0.223

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB Difference from Current Entry 8BTS Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
8P8G Nitrogenase MoFe protein from A. vinelandii beta double mutant D353G/D357G Deposited 2023-06-01 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain A 3–492（490 aa）
Chain C 3–492（490 aa）
Not recorded EDO 1,2-ETHANEDIOL × 35 CL CHLORIDE ION × 2 HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 2 ICS iron-sulfur-molybdenum cluster with interstitial carbon × 2 DIO 1,4-DIETHYLENE DIOXIDE × 2 GOL GLYCEROL × 1 1CL FE(8)-S(7) CLUSTER, OXIDIZED × 2 CLF FE(8)-S(7) CLUSTER × 2 NA SODIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.6；293.15 K；The beta-D353G/D357G MoFe-protein was crystallized anaerobically at 17.5 mg/mL under 100% N2 atmosphere. The protein was spotted as a sitting drop to 96-Well MRC 2-Drop polystyrene Crystallization Plates (SWISSCI) containing 90 uL of crystallization solution in the reservoir. Each drop contained 0.5 uL of protein sample and 0.5 uL of crystallization solution. Crystals were obtained in the crystallization solution containing 10 % w/v Polyethylene glycol 10,000; 2 % v/v 1,4-Dioxane; 100 mM tri-Sodium citrate; pH 5.6, and 1 mM polyoxotungstate [TeW6O24]6- (TEW). Sealed plates were stored inside a Coy anaerobic chamber filled with an atmosphere of N2:H2 97:3 at 20 C. Crystals were soaked in the crystallization solution supplemented with 30% v/v ethylene glycol for a few seconds before freezing in liquid nitrogen.
Resolution 1.55 Å R-free 0.187

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name C1DGZ7_AZOVD
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 11–500； UniProt 3–492 Author chain C； PDBConstruct 11–500； UniProt 3–492 Author chain H； PDBConstruct 11–500； UniProt 3–492 Author chain J； PDBConstruct 11–500； UniProt 3–492

Nitrogenase molybdenum-iron protein beta chain

Azotobacter vinelandii DJ

UniProt P07329

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count Chain B； UniProt 1–523 Chain D； UniProt 1–523 Not recorded Nitrogenase protein alpha chain × 2 （C1DGZ7） HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 2 ICS iron-sulfur-molybdenum cluster with interstitial carbon × 2 GOL GLYCEROL × 10 SO4 SULFATE ION × 5 1CL FE(8)-S(7) CLUSTER, OXIDIZED × 2 FE FE (III) ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 5.5；293.15 K；The purified enzyme in 50 mM Tris/HCl pH 8.0, 300 mM NaCl, 2 mM dithionite was crystallized at 8 mg.ml-1. Crystallization was performed anaerobically in a tent containing 100 % N2 atmosphere. Crystals were obtained by initial screening at 20 degree Celsius on 96-Well MRC 2-drop crystallization plates in polystyrene (SWISSCI) containing 90 ul of crystallization solution in the reservoir. The protein sample (0.5 ul) was mixed with 0.5 ul reservoir solution. The reservoir solution contained 25 % w/v Polyethylene glycol 3,350, 100 mM BIS-TRIS at pH 5.5, and 200 mM Lithium sulfate. The plate was then incubated in a Coy tent (N2/H2, 97:3) at 20 degree Celsius. Crystals appeared after a few weeks and were soaked in the crystallization solution supplemented with 15 % v/v glycerol as a cryo-protectant before being frozen in liquid nitrogen. Resolution 3.03 Å R-free 0.223
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count Chain I； UniProt 1–523 Chain L； UniProt 1–523 Not recorded Nitrogenase protein alpha chain × 2 （C1DGZ7） HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 2 ICS iron-sulfur-molybdenum cluster with interstitial carbon × 2 GOL GLYCEROL × 2 SO4 SULFATE ION × 5 1CL FE(8)-S(7) CLUSTER, OXIDIZED × 2 FE FE (III) ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 5.5；293.15 K；The purified enzyme in 50 mM Tris/HCl pH 8.0, 300 mM NaCl, 2 mM dithionite was crystallized at 8 mg.ml-1. Crystallization was performed anaerobically in a tent containing 100 % N2 atmosphere. Crystals were obtained by initial screening at 20 degree Celsius on 96-Well MRC 2-drop crystallization plates in polystyrene (SWISSCI) containing 90 ul of crystallization solution in the reservoir. The protein sample (0.5 ul) was mixed with 0.5 ul reservoir solution. The reservoir solution contained 25 % w/v Polyethylene glycol 3,350, 100 mM BIS-TRIS at pH 5.5, and 200 mM Lithium sulfate. The plate was then incubated in a Coy tent (N2/H2, 97:3) at 20 degree Celsius. Crystals appeared after a few weeks and were soaked in the crystallization solution supplemented with 15 % v/v glycerol as a cryo-protectant before being frozen in liquid nitrogen. Resolution 3.03 Å R-free 0.223

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB Difference from Current Entry 8BTS Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
11NA Azotobacter vinelandii MoFeP (C1 symmetry) determined using the SPT Labtech chameleon in the presence of 0x SurfACT Deposited 2026-03-05 Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 1–523（523 aa）
Chain D 1–523（523 aa）
Not recorded HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 2 ICS iron-sulfur-molybdenum cluster with interstitial carbon × 2 CLF FE(8)-S(7) CLUSTER × 2 FE FE (III) ION × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE；Samples were frozen with the SPT Labtech chameleon
Resolution 2.69 Å
11NB Azotobacter vinelandii MoFeP (C2 symmetry) determined using the SPT Labtech chameleon in the presence of 0x SurfACT Deposited 2026-03-05 Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 1–523（523 aa）
Chain D 1–523（523 aa）
Not recorded HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 2 ICS iron-sulfur-molybdenum cluster with interstitial carbon × 2 FE FE (III) ION × 2 CLF FE(8)-S(7) CLUSTER × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE；Samples were frozen with the SPT Labtech chameleon
Resolution 2.46 Å
11NC Azotobacter vinelandii MoFeP (C1 symmetry) determined using the SPT Labtech chameleon in the presence of 0.25x SurfACT Deposited 2026-03-05 Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 1–523（523 aa）
Chain D 1–523（523 aa）
Not recorded HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 2 ICS iron-sulfur-molybdenum cluster with interstitial carbon × 2 FE FE (III) ION × 2 CLF FE(8)-S(7) CLUSTER × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE；Samples were frozen with the SPT Labtech chameleon
Resolution 2.16 Å
11ND Azotobacter vinelandii MoFeP (C2 symmetry) determined using the SPT Labtech chameleon in the presence of 0.25x SurfACT Deposited 2026-03-05 Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 1–523（523 aa）
Chain D 1–523（523 aa）
Not recorded HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 2 ICS iron-sulfur-molybdenum cluster with interstitial carbon × 2 FE FE (III) ION × 2 CLF FE(8)-S(7) CLUSTER × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE；Samples were frozen with the SPT Labtech chameleon
Resolution 2.06 Å
11NE Azotobacter vinelandii MoFeP (C1 symmetry) determined using the SPT Labtech chameleon in the presence of 1x SurfACT Deposited 2026-03-05 Different construct Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 2–523（522 aa）
Chain D 2–523（522 aa）
Not recorded HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 2 ICS iron-sulfur-molybdenum cluster with interstitial carbon × 2 FE FE (III) ION × 2 CLF FE(8)-S(7) CLUSTER × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE；Samples were frozen with the SPT Labtech chameleon
Resolution 2.49 Å
11NF Azotobacter vinelandii MoFeP (C2 symmetry) determined using the SPT Labtech chameleon in the presence of 1x SurfACT Deposited 2026-03-05 Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 1–523（523 aa）
Chain D 1–523（523 aa）
Not recorded HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 2 ICS iron-sulfur-molybdenum cluster with interstitial carbon × 2 FE FE (III) ION × 2 CLF FE(8)-S(7) CLUSTER × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE；Samples were frozen with the SPT Labtech chameleon
Resolution 2.34 Å
1FP4 CRYSTAL STRUCTURE OF THE ALPHA-H195Q MUTANT OF NITROGENASE Deposited 2000-08-30 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 1–523（523 aa）
Chain D 1–523（523 aa）
Not recorded HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 2 CFM FE-MO-S CLUSTER × 2 CLP FE-S CLUSTER × 2 CA CALCIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions microcapillary batch diffusion；pH 8；298 K；PEG 4000, TRIS pH 8.0, sodium molybdate, microcapillary batch diffusion, temperature 298K
Resolution 2.50 Å R-free 0.240
1G20 MGATP-BOUND AND NUCLEOTIDE-FREE STRUCTURES OF A NITROGENASE PROTEIN COMPLEX BETWEEN LEU127DEL-FE PROTEIN AND THE MOFE PROTEIN Deposited 2000-10-16 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric
Chain B 1–522（522 aa）
Chain D 1–522（522 aa）
Not recorded HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 2 CFM FE-MO-S CLUSTER × 2 CA CALCIUM ION × 2 CLF FE(8)-S(7) CLUSTER × 2 SF4 IRON/SULFUR CLUSTER × 2 X-RAY DIFFRACTION
X-ray crystallization conditions microcapillary batch diffusion；pH 8.5；298 K；PEG 4000, sodium acetate, Tris-HCl. Ph 8.8, pH 8.5, microcapillary batch diffusion, temperature 298K
Resolution 2.20 Å R-free 0.255
1G21 MGATP-BOUND AND NUCLEOTIDE-FREE STRUCTURES OF A NITROGENASE PROTEIN COMPLEX BETWEEN LEU127DEL-FE PROTEIN AND THE MOFE PROTEIN Deposited 2000-10-16 Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric
Chain B 1–523（523 aa）
Chain D 1–523（523 aa）
Not recorded HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 2 CFM FE-MO-S CLUSTER × 2 CLF FE(8)-S(7) CLUSTER × 2 CA CALCIUM ION × 2 MG MAGNESIUM ION × 4 ATP ADENOSINE-5'-TRIPHOSPHATE × 4 SF4 IRON/SULFUR CLUSTER × 2 X-RAY DIFFRACTION
X-ray crystallization conditions microcapillary batch diffusion；pH 8.5；298 K；PEG 4000, sodium acetate, Tris-HCl. Ph 8.8, pH 8.5, microcapillary batch diffusion, temperature 298K
Resolution 3.00 Å R-free 0.285
1L5H FeMo-cofactor Deficient Nitrogenase MoFe Protein Deposited 2002-03-06 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 1–522（522 aa）
Not recorded CA CALCIUM ION × 2 CLF FE(8)-S(7) CLUSTER × 2 X-RAY DIFFRACTION
X-ray crystallization conditions LIQUID DIFFUSION；pH 9.5；298 K；PEG 8000, CHES, pH 9.5, LIQUID DIFFUSION, temperature 298K
Resolution 2.30 Å R-free 0.289
1M1N Nitrogenase MoFe protein from Azotobacter vinelandii Deposited 2002-06-19 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 1–522（522 aa）
Chain D 1–522（522 aa）
Not recorded HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 2 CFN FE(7)-MO-S(9)-N CLUSTER × 2 CA CALCIUM ION × 2 CLF FE(8)-S(7) CLUSTER × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；298 K；PEG 8000, sodium chloride, TRIS, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 298K
Resolution 1.16 Å R-free 0.149
1M1N Nitrogenase MoFe protein from Azotobacter vinelandii Deposited 2002-06-19 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain F 1–522（522 aa）
Chain H 1–522（522 aa）
Not recorded HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 2 CFN FE(7)-MO-S(9)-N CLUSTER × 2 CA CALCIUM ION × 2 CLF FE(8)-S(7) CLUSTER × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；298 K；PEG 8000, sodium chloride, TRIS, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 298K
Resolution 1.16 Å R-free 0.149
1M1Y Chemical Crosslink of Nitrogenase MoFe Protein and Fe Protein Deposited 2002-06-20 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric
Chain B 1–522（522 aa）
Chain D 1–522（522 aa）
Not recorded HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 2 CFM FE-MO-S CLUSTER × 2 CLF FE(8)-S(7) CLUSTER × 2 CA CALCIUM ION × 2 SF4 IRON/SULFUR CLUSTER × 2 X-RAY DIFFRACTION
X-ray crystallization conditions LIQUID DIFFUSION；pH 8；298 K；PEG 6000, NaCl, Cadaverine, Tris, pH 8.0, LIQUID DIFFUSION, temperature 298K
Resolution 3.20 Å R-free 0.329
1M1Y Chemical Crosslink of Nitrogenase MoFe Protein and Fe Protein Deposited 2002-06-20 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric
Chain J 1–522（522 aa）
Chain L 1–522（522 aa）
Not recorded HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 2 CFM FE-MO-S CLUSTER × 2 CLF FE(8)-S(7) CLUSTER × 2 CA CALCIUM ION × 2 SF4 IRON/SULFUR CLUSTER × 2 X-RAY DIFFRACTION
X-ray crystallization conditions LIQUID DIFFUSION；pH 8；298 K；PEG 6000, NaCl, Cadaverine, Tris, pH 8.0, LIQUID DIFFUSION, temperature 298K
Resolution 3.20 Å R-free 0.329
1N2C NITROGENASE COMPLEX FROM AZOTOBACTER VINELANDII STABILIZED BY ADP-TETRAFLUOROALUMINATE Deposited 1997-05-02 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric
Chain B 1–522（522 aa） Fragment：CHAINS A AND C ARE THE ALPHA CHAINS, CHAINS B AND D ARE THE BETA CHAINS
Chain D 1–522（522 aa） Fragment：CHAINS A AND C ARE THE ALPHA CHAINS, CHAINS B AND D ARE THE BETA CHAINS
Not recorded HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 2 CFM FE-MO-S CLUSTER × 2 CA CALCIUM ION × 2 CLF FE(8)-S(7) CLUSTER × 2 MG MAGNESIUM ION × 4 ALF TETRAFLUOROALUMINATE ION × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 4 SF4 IRON/SULFUR CLUSTER × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.5；16-20% PEG 8000, 0.1 M CACODYLATE PH 6.5 AND 20-50 MM MGCL2
Resolution 3.00 Å R-free 0.238
2AFH Crystal Structure of Nucleotide-Free Av2-Av1 Complex Deposited 2005-07-25 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric
Chain B 1–522（522 aa）
Chain D 1–522（522 aa）
Not recorded HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 2 CFN FE(7)-MO-S(9)-N CLUSTER × 2 PGE TRIETHYLENE GLYCOL × 8 CA CALCIUM ION × 2 NA SODIUM ION × 1 CLF FE(8)-S(7) CLUSTER × 2 TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 2 PG4 TETRAETHYLENE GLYCOL × 2 1PE PENTAETHYLENE GLYCOL × 2 PEG DI(HYDROXYETHYL)ETHER × 3 P6G HEXAETHYLENE GLYCOL × 1 SF4 IRON/SULFUR CLUSTER × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；298 K；PEG 10000, Tris, sodium chloride, magnesium chloride, dithionite, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 298 K
Resolution 2.10 Å R-free 0.221
2AFI Crystal Structure of MgADP bound Av2-Av1 Complex Deposited 2005-07-25 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric
Chain B 1–522（522 aa）
Chain D 1–522（522 aa）
Not recorded HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 2 CFN FE(7)-MO-S(9)-N CLUSTER × 2 CA CALCIUM ION × 2 CLF FE(8)-S(7) CLUSTER × 2 MG MAGNESIUM ION × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 4 SF4 IRON/SULFUR CLUSTER × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；298 K；PEG8000, Sodium Chloride, Magnesium Chloride, ADP, Dithionite, TRIS, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 298 K
Resolution 3.10 Å R-free 0.270
2AFI Crystal Structure of MgADP bound Av2-Av1 Complex Deposited 2005-07-25 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric
Chain J 1–522（522 aa）
Chain L 1–522（522 aa）
Not recorded HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 2 CFN FE(7)-MO-S(9)-N CLUSTER × 2 CA CALCIUM ION × 2 CLF FE(8)-S(7) CLUSTER × 2 MG MAGNESIUM ION × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 4 SF4 IRON/SULFUR CLUSTER × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；298 K；PEG8000, Sodium Chloride, Magnesium Chloride, ADP, Dithionite, TRIS, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 298 K
Resolution 3.10 Å R-free 0.270
2MIN NITROGENASE MOFE PROTEIN FROM AZOTOBACTER VINELANDII, OXIDIZED STATE Deposited 1996-12-20 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 1–522（522 aa）
Chain D 1–522（522 aa）
Not recorded HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 2 CLF FE(8)-S(7) CLUSTER × 2 CFM FE-MO-S CLUSTER × 2 CA CALCIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 8.5；PROTEIN WAS CRYSTALLIZED USING PRECIPITATING SOLUTION OF 30% PEG 4000, 0.2M NA2MO4, 0.1M TRIS PH 8.5
Resolution 2.03 Å R-free 0.266
3K1A Insights into substrate binding at FeMo-cofactor in nitrogenase from the structure of an alpha-70Ile MoFe protein variant Deposited 2009-09-26 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 2–523（522 aa）
Chain D 2–523（522 aa）
Not recorded HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 2 CFN FE(7)-MO-S(9)-N CLUSTER × 2 CLF FE(8)-S(7) CLUSTER × 2 CA CALCIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions LIQUID DIFFUSION；pH 8；298 K；30% PEG 4000, 100mM Tris-HCl pH 8.0, 170-190mM Sodium molybdate and 1mM Dithionite, LIQUID DIFFUSION, temperature 298.0K
Resolution 2.23 Å R-free 0.254
3MIN NITROGENASE MOFE PROTEIN FROM AZOTOBACTER VINELANDII, OXIDIZED STATE Deposited 1996-12-20 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 1–522（522 aa）
Chain D 1–522（522 aa）
Not recorded HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 2 CFM FE-MO-S CLUSTER × 2 CA CALCIUM ION × 2 CLF FE(8)-S(7) CLUSTER × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 8.5；PROTEIN WAS CRYSTALLIZED USING PRECIPITATING SOLUTION OF 30% PEG 4000, 0.2M NA2MO4, 0.1M TRIS PH 8.5 SOAKED IN SOAKED IN SODIUM DITHIONITE, 10MM FINAL CONC.
Resolution 2.03 Å R-free 0.264
3U7Q A. vinelandii nitrogenase MoFe protein at atomic resolution Deposited 2011-10-14 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 1–523（523 aa）
Chain D 1–523（523 aa）
Not recorded HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 2 ICS iron-sulfur-molybdenum cluster with interstitial carbon × 2 IMD IMIDAZOLE × 8 CA CALCIUM ION × 2 1CL FE(8)-S(7) CLUSTER, OXIDIZED × 2 CLF FE(8)-S(7) CLUSTER × 2 MG MAGNESIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；291 K；16.5% v/v PEG6000, 0.55 M sodium chloride, 12.5% v/v MPD, 1.5% v/v xylitol, 0.2 M imidazole/malate buffer, pH 8.0, 0.1 mM Zwittergent 3-14, 0.55 mM spermine, VAPOR DIFFUSION, SITTING DROP, temperature 291K
Resolution 1.00 Å R-free 0.146
4ND8 Av Nitrogenase MoFe Protein High pH Form Deposited 2013-10-25 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 1–523（523 aa）
Chain D 1–523（523 aa）
Not recorded HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 2 ICS iron-sulfur-molybdenum cluster with interstitial carbon × 2 1CL FE(8)-S(7) CLUSTER, OXIDIZED × 2 FE FE (III) ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 9.79；295 K；150 mM ACES, 75 mM Tris and 75 mM ethanolamine, pH 9.79, 17%-18% PEG 3350, 0.8 M NaCl, 1 mM sodium dithionite, VAPOR DIFFUSION, temperature 295.K
Resolution 2.00 Å R-free 0.204
4TKU Reactivated Nitrogenase MoFe-protein from A. vinelandii Deposited 2014-05-27 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 1–523（523 aa）
Chain D 1–523（523 aa）
Not recorded HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 2 ICS iron-sulfur-molybdenum cluster with interstitial carbon × 2 IMD IMIDAZOLE × 8 CL CHLORIDE ION × 2 CLF FE(8)-S(7) CLUSTER × 2 FE2 FE (II) ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；294 K；PEG4000, NaCl, imidazole/malate, glycerol, sodium dithionite
Resolution 1.43 Å R-free 0.142
4TKV CO-bound Nitrogenase MoFe-protein from A. vinelandii Deposited 2014-05-28 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 1–523（523 aa）
Chain D 1–523（523 aa）
Not recorded HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 2 ICE iron-sulfur-molybdenum cluster with interstitial carbon × 4 IMD IMIDAZOLE × 8 CMO CARBON MONOXIDE × 6 CLF FE(8)-S(7) CLUSTER × 2 FE2 FE (II) ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；294 K；PEG4000, NaCl, imidazole/malate, Glycerol, sodium dithionite
Resolution 1.50 Å R-free 0.154
4WNA Structure of the Nitrogenase MoFe Protein from Azotobacter vinelandii Pressurized with Xenon Deposited 2014-10-11 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 1–523（523 aa）
Chain D 1–523（523 aa）
Not recorded HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 2 ICS iron-sulfur-molybdenum cluster with interstitial carbon × 2 CLF FE(8)-S(7) CLUSTER × 2 XE XENON × 6 FE FE (III) ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；297 K；PEG 6000, sodium chloride, xylitol, imidazole/malate, spermine, Zwittergent
Resolution 2.00 Å R-free 0.219
4WZA Asymmetric Nucleotide Binding in the Nitrogenase Complex Deposited 2014-11-19 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric
Chain B 2–523（522 aa）
Chain D 2–523（522 aa）
Not recorded HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 2 ICS iron-sulfur-molybdenum cluster with interstitial carbon × 2 CLF FE(8)-S(7) CLUSTER × 2 FE FE (III) ION × 2 SF4 IRON/SULFUR CLUSTER × 2 MG MAGNESIUM ION × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；298 K；18-22% PEG 8000, 0-50 mM NaCl, 100 mM Tris pH 8.5, 10 mM sodium dithionite, 10 mM MgCl2, 5 mM AMPPCP, 5 mM ADP
Resolution 1.90 Å R-free 0.187
4WZB Crystal Structure of MgAMPPCP-bound Av2-Av1 complex Deposited 2014-11-19 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric
Chain B 2–523（522 aa）
Chain D 2–523（522 aa）
Not recorded HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 2 ICS iron-sulfur-molybdenum cluster with interstitial carbon × 2 CLF FE(8)-S(7) CLUSTER × 2 FE2 FE (II) ION × 2 MG MAGNESIUM ION × 4 ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER × 4 SF4 IRON/SULFUR CLUSTER × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；298 K；PEG 8000, TRIS, SODIUM CHLORIDE, MAGNESIUM CHLORIDE, DITHIONITE, AMPPCP, PH 8.5
Resolution 2.30 Å R-free 0.255
4XPI Fe protein independent substrate reduction by nitrogenase variants altered in intramolecular electron transfer Deposited 2015-01-17 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 2–523（522 aa）
Chain D 2–523（522 aa）
Mutation：Y98H Mutation：Y98H HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 2 ICS iron-sulfur-molybdenum cluster with interstitial carbon × 2 GOL GLYCEROL × 15 1CL FE(8)-S(7) CLUSTER, OXIDIZED × 2 CA CALCIUM ION × 2 TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions LIQUID DIFFUSION；pH 8；298 K；30% PEG 4000, 100mM Tris-HCl pH 8.0, 170-190mM Sodium molybdate and 1mM Dithionite, LIQUID DIFFUSION, temperature 298.0K
Resolution 1.97 Å R-free 0.264
5BVG Selenium incorporated nitrogenase MoFe-protein (Av1-Se2B) from A. vinelandii Deposited 2015-06-05 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 1–523（523 aa）
Chain D 1–523（523 aa）
Not recorded HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 2 ICG iron-sulfur-molybdenum cluster with interstitial carbon with selenium incorporated × 2 IMD IMIDAZOLE × 9 CL CHLORIDE ION × 2 CLF FE(8)-S(7) CLUSTER × 2 FE2 FE (II) ION × 2 SE SELENIUM ATOM × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；291 K；PEG 8000, NaCl, Imidazole/Malate, Sodiumdithionite
Resolution 1.60 Å R-free 0.179
5BVH CO-bound form of Selenium incorporated nitrogenase MoFe-protein (Av1-Se-CO) from A. vinelandii Deposited 2015-06-05 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 1–523（523 aa）
Chain D 1–523（523 aa）
Not recorded HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 2 ICS iron-sulfur-molybdenum cluster with interstitial carbon × 2 ICH iron-sulfur-molybdenum cluster with interstitial carbon with selenium incorporated × 2 IMD IMIDAZOLE × 8 CL CHLORIDE ION × 2 CMO CARBON MONOXIDE × 2 CLF FE(8)-S(7) CLUSTER × 2 FE2 FE (II) ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；291 K；PEG 8000, NaCl, Imidazole/Malate, Sodiumdithionite
Resolution 1.53 Å R-free 0.160
5CX1 Nitrogenase molybdenum-iron protein beta-K400E mutant Deposited 2015-07-28 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 1–523（523 aa）
Chain D 1–523（523 aa）
Mutation：K400D Mutation：K400D HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 2 ICS iron-sulfur-molybdenum cluster with interstitial carbon × 2 CLF FE(8)-S(7) CLUSTER × 2 CA CALCIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；293 K；100 mM Tris pH 8, 600 mM NaCl, 18% PEG 10000, 5 mM sodium dithionite
Resolution 1.75 Å R-free 0.245
5CX1 Nitrogenase molybdenum-iron protein beta-K400E mutant Deposited 2015-07-28 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain F 1–523（523 aa）
Chain H 1–523（523 aa）
Mutation：K400D Mutation：K400D HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 2 ICS iron-sulfur-molybdenum cluster with interstitial carbon × 2 CLF FE(8)-S(7) CLUSTER × 2 CA CALCIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；293 K；100 mM Tris pH 8, 600 mM NaCl, 18% PEG 10000, 5 mM sodium dithionite
Resolution 1.75 Å R-free 0.245
5CX1 Nitrogenase molybdenum-iron protein beta-K400E mutant Deposited 2015-07-28 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain J 1–523（523 aa）
Chain L 1–523（523 aa）
Mutation：K400D Mutation：K400D HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 2 ICS iron-sulfur-molybdenum cluster with interstitial carbon × 2 CLF FE(8)-S(7) CLUSTER × 2 CA CALCIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；293 K；100 mM Tris pH 8, 600 mM NaCl, 18% PEG 10000, 5 mM sodium dithionite
Resolution 1.75 Å R-free 0.245
5CX1 Nitrogenase molybdenum-iron protein beta-K400E mutant Deposited 2015-07-28 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain N 1–523（523 aa）
Chain P 1–523（523 aa）
Mutation：K400D Mutation：K400D HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 2 ICS iron-sulfur-molybdenum cluster with interstitial carbon × 2 CLF FE(8)-S(7) CLUSTER × 2 CA CALCIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；293 K；100 mM Tris pH 8, 600 mM NaCl, 18% PEG 10000, 5 mM sodium dithionite
Resolution 1.75 Å R-free 0.245
5VQ4 Nitrogenase Av1 at pH 5 Deposited 2017-05-07 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 1–523（523 aa）
Chain D 1–523（523 aa）
Not recorded HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 2 ICS iron-sulfur-molybdenum cluster with interstitial carbon × 2 CLF FE(8)-S(7) CLUSTER × 2 FE FE (III) ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；PEG 4000, sodium chloride, imidazole/malate, sodium dithionite
Resolution 2.30 Å R-free 0.222
6BBL Crystal structure of the a-96Gln MoFe protein variant in the presence of the substrate acetylene Deposited 2017-10-18 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 1–523（523 aa）
Chain D 1–523（523 aa）
Not recorded C2H acetylene × 2 IMD IMIDAZOLE × 3 HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 2 ICS iron-sulfur-molybdenum cluster with interstitial carbon × 2 1CL FE(8)-S(7) CLUSTER, OXIDIZED × 2 FE FE (III) ION × 2 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions MICROBATCH；pH 8；295 K；30% w/v PEG4000, 0.1 M Tris, pH 8.0, 0.17 M sodium molybdate, 0.001 M sodium dithionite
Resolution 1.68 Å R-free 0.185
6CDK Characterization of the P1+ intermediate state of nitrogenase P-cluster Deposited 2018-02-08 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 1–523（523 aa）
Chain D 1–523（523 aa）
Not recorded HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 2 ICS iron-sulfur-molybdenum cluster with interstitial carbon × 2 CLF FE(8)-S(7) CLUSTER × 2 FE FE (III) ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions LIQUID DIFFUSION；pH 8；298 K；30% PEG4000, 100 mM Tris-HCl, pH 8.0, 170-190 mM sodium molybdate, 1 mM dithionite
Resolution 2.10 Å R-free 0.263
6O7L Nitrogenase MoFeP mutant S188A from Azotobacter vinelandii in the dithionite reduced state after redox cycling Deposited 2019-03-08 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 1–523（523 aa）
Chain D 1–523（523 aa）
Mutation：S188A Mutation：S188A HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 2 ICS iron-sulfur-molybdenum cluster with interstitial carbon × 2 CLF FE(8)-S(7) CLUSTER × 2 FE FE (III) ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；18% PEG 8000, 100 mM Tris pH 7.5, 500 mM NaCl, 10 mM dithionite
Resolution 2.26 Å R-free 0.254
6O7M Nitrogenase MoFeP mutant F99Y from Azotobacter vinelandii in the indigo carmine oxidized state Deposited 2019-03-08 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 1–523（523 aa）
Chain D 1–523（523 aa）
Mutation：F99Y Mutation：F99Y HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 2 ICS iron-sulfur-molybdenum cluster with interstitial carbon × 2 CLF FE(8)-S(7) CLUSTER × 2 FE FE (III) ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.3；293 K；18% PEG 8000, 100 mM Tris pH 8.3, 500 mM NaCl, 5 mM indigo carmine (IDS)
Resolution 1.40 Å R-free 0.208
6O7N Nitrogenase MoFeP mutant F99Y/S188A from Azotobacter vinelandii in the indigo carmine oxidized state Deposited 2019-03-08 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 1–523（523 aa）
Chain D 1–523（523 aa）
Mutation：F99Y, S188A Mutation：F99Y, S188A HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 2 ICS iron-sulfur-molybdenum cluster with interstitial carbon × 2 CLF FE(8)-S(7) CLUSTER × 2 FE FE (III) ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.8；293 K；18% PEG 8000, 100 mM Tris pH 7.8, 500 mM NaCl, 5 mM indigo carmine
Resolution 1.75 Å R-free 0.223
6O7O Nitrogenase MoFeP mutant F99Y/S188A from Azotobacter vinelandii in the dithionite reduced state after redox cycling Deposited 2019-03-08 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 1–523（523 aa）
Chain D 1–523（523 aa）
Mutation：F99Y, S188A Mutation：F99Y, S188A HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 2 ICS iron-sulfur-molybdenum cluster with interstitial carbon × 2 CLF FE(8)-S(7) CLUSTER × 2 FE FE (III) ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；293 K；18% PEG 8000, 100 mM Tris pH 8.5, 500 mM NaCl, 10 mM dithionite. Protein was redox cycled with 5 mM indigo carmine and 10 mM dithionite prior to crystallization.
Resolution 1.89 Å R-free 0.186
6O7P Nitrogenase MoFeP mutant F99Y from Azotobacter vinelandii in the dithionite reduced state Deposited 2019-03-08 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 1–523（523 aa）
Chain D 1–523（523 aa）
Mutation：F99Y Mutation：F99Y HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 2 ICS iron-sulfur-molybdenum cluster with interstitial carbon × 2 CLF FE(8)-S(7) CLUSTER × 2 FE FE (III) ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.3；293 K；22% PEG 8000, 100 mM Tris pH 8.3, 500 mM NaCl, 10 mM dithionite
Resolution 1.70 Å R-free 0.201
6O7Q Nitrogenase MoFeP mutant S188A from Azotobacter vinelandii in the dithionite reduced state after redox cycling Deposited 2019-03-08 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 1–523（523 aa）
Chain D 1–523（523 aa）
Mutation：S188A Mutation：S188A CLF FE(8)-S(7) CLUSTER × 2 HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 2 ICS iron-sulfur-molybdenum cluster with interstitial carbon × 2 FE FE (III) ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；293 K；20% PEG 8000, 100 mM Tris pH 8.0, 500 mM NaCl, 10 mM dithionite. Protein was redox cycled with 5 mM indigo carmine and 10 mM dithionite prior to crystallization.
Resolution 2.00 Å R-free 0.229
6O7R Nitrogenase MoFeP mutant F99Y, S188A from Azotobacter vinelandii in the dithionite reduced state Deposited 2019-03-08 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 1–523（523 aa）
Chain D 1–523（523 aa）
Mutation：F99Y, S188A Mutation：F99Y, S188A HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 2 ICS iron-sulfur-molybdenum cluster with interstitial carbon × 2 CLF FE(8)-S(7) CLUSTER × 2 FE FE (III) ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；293 K；20% PEG 8000, 100 mM Tris pH 8.0, 500 mM NaCl, 10 mM dithionite
Resolution 2.27 Å R-free 0.208
6O7S Nitrogenase MoFeP mutant S188A from Azotobacter vinelandii in the indigo carmine oxidized state Deposited 2019-03-08 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 1–523（523 aa）
Chain D 1–523（523 aa）
Mutation：S188A Mutation：S188A HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 2 ICS iron-sulfur-molybdenum cluster with interstitial carbon × 2 NA SODIUM ION × 2 LPJ FE(6)-S(7) CLUSTER × 2 FE FE (III) ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；293 K；20% PEG 8000, 100 mM Tris pH 8.0, 500 mM NaCl
Resolution 2.27 Å R-free 0.208
6OP1 Selenium incorporated, carbon monoxide inhibited FeMo-cofactor of azotobacter vinelandii Deposited 2019-04-24 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 2–523（522 aa）
Chain D 2–523（522 aa）
Not recorded HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 2 ICS iron-sulfur-molybdenum cluster with interstitial carbon × 2 IMD IMIDAZOLE × 9 CMO CARBON MONOXIDE × 2 MG MAGNESIUM ION × 5 CLF FE(8)-S(7) CLUSTER × 2 CA CALCIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；291 K；26% v/v PEG6000, 0.75 M sodium chloride, 12.5% v/v MPD, 0.1 M imidazole/malate buffer, pH 8.0, 5 mM Na2S2O4
Resolution 1.70 Å R-free 0.165
6OP2 Selenium incorporated FeMo-cofactor of nitrogenase from azotobacter vinelandii at high concentration of selenium Deposited 2019-04-24 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 2–523（522 aa）
Chain D 2–523（522 aa）
Not recorded HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 2 ICS iron-sulfur-molybdenum cluster with interstitial carbon × 2 IMD IMIDAZOLE × 11 SE SELENIUM ATOM × 2 CA CALCIUM ION × 2 CLF FE(8)-S(7) CLUSTER × 2 MG MAGNESIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；291 K；26% v/v PEG6000, 0.75 M sodium chloride, 12.5% v/v MPD, 0.1 M imidazole/malate buffer, pH 8.0, 5 mM Na2S2O4
Resolution 1.90 Å R-free 0.214
6OP3 Selenium incorporated FeMo-cofactor of nitrogenase from Azotobacter vinelandii with low concentration of selenium Deposited 2019-04-24 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 2–523（522 aa）
Chain D 2–523（522 aa）
Not recorded HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 2 ICS iron-sulfur-molybdenum cluster with interstitial carbon × 2 IMD IMIDAZOLE × 12 SE SELENIUM ATOM × 2 CLF FE(8)-S(7) CLUSTER × 2 MG MAGNESIUM ION × 2 CA CALCIUM ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；291 K；26% v/v PEG6000, 0.75 M sodium chloride, 12.5% v/v MPD, 0.1 M imidazole/malate buffer, pH 8.0, 5 mM Na2S2O4
Resolution 1.60 Å R-free 0.152
6OP4 Selenium-incorporated, carbon monoxide-inhibited, reactivated FeMo-cofactor of nitrogenase from Azotobacter vinelandii Deposited 2019-04-24 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 2–523（522 aa）
Chain D 2–523（522 aa）
Not recorded HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 2 ICS iron-sulfur-molybdenum cluster with interstitial carbon × 2 IMD IMIDAZOLE × 9 CLF FE(8)-S(7) CLUSTER × 2 CA CALCIUM ION × 2 MG MAGNESIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；291 K；26% v/v PEG6000, 0.75 M sodium chloride, 12.5% v/v MPD, 0.1 M imidazole/malate buffer, pH 8.0, 5 mM Na2S2O4
Resolution 2.30 Å R-free 0.223
6UG0 N2-bound Nitrogenase MoFe-protein from Azotobacter vinelandii Deposited 2019-09-25 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 1–523（523 aa）
Chain D 1–523（523 aa）
Not recorded HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 2 ICE iron-sulfur-molybdenum cluster with interstitial carbon × 1 HDZ NITROGEN MOLECULE × 3 H2S HYDROSULFURIC ACID × 6 MO MOLYBDENUM ATOM × 8 1CL FE(8)-S(7) CLUSTER, OXIDIZED × 2 FE FE (III) ION × 2 GOL GLYCEROL × 6 PGE TRIETHYLENE GLYCOL × 1 ICZ iron-sulfur-molybdenum cluster with interstitial carbon × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；293 K；14-19 % w/v PEG smear high, 0.16M ammonium acetate, 0.1M sodium citrate (pH 5.0), 25.6 % v/v glycerol, 5mM Eu(II)-EGTA
Resolution 1.83 Å R-free 0.259
6VXT Activated Nitrogenase MoFe-protein from Azotobacter vinelandii Deposited 2020-02-24 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 1–523（523 aa）
Chain D 1–523（523 aa）
Not recorded HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 2 ICS iron-sulfur-molybdenum cluster with interstitial carbon × 2 MO MOLYBDENUM ATOM × 8 H2S HYDROSULFURIC ACID × 2 CLF FE(8)-S(7) CLUSTER × 2 FE FE (III) ION × 2 GOL GLYCEROL × 7 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；293 K；14-19 % w/v PEG smear high, 0.16 M ammonium acetate, 0.1 M sodium citrate(pH 5.0), 25.6 % v/v glycerol, 5 mM sodium dithionite
Resolution 1.74 Å R-free 0.203
7JRF CO-CO-BOUND NITROGENASE MOFE-PROTEIN FROM A. VINELANDII Deposited 2020-08-12 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 1–523（523 aa）
Chain D 1–523（523 aa）
Not recorded HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 2 ICE iron-sulfur-molybdenum cluster with interstitial carbon × 2 IMD IMIDAZOLE × 8 H2S HYDROSULFURIC ACID × 2 CMO CARBON MONOXIDE × 4 CLF FE(8)-S(7) CLUSTER × 2 CA CALCIUM ION × 2 MG MAGNESIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；Peg 4000, sodium chloride, imidazole / malate, glycerol, spermine
Resolution 1.33 Å R-free 0.150
8CRS CryoEM Structure of nitrogenase MoFe-protein in detergent Deposited 2022-05-11 Different construct Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 2–523（522 aa）
Chain D 2–523（522 aa）
Not recorded ICS iron-sulfur-molybdenum cluster with interstitial carbon × 2 HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 2 1N7 CHAPSO × 4 CLF FE(8)-S(7) CLUSTER × 2 FE FE (III) ION × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.8
cryo-EM vitrification conditions Cryogen ETHANE-PROPANE
Resolution 2.04 Å
8DBX CryoEM structure of partially oxidized MoFe-protein on ultrathin carbon Deposited 2022-06-14 Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 1–523（523 aa）
Chain D 1–523（523 aa）
Not recorded ICS iron-sulfur-molybdenum cluster with interstitial carbon × 2 HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 2 CLF FE(8)-S(7) CLUSTER × 2 1CL FE(8)-S(7) CLUSTER, OXIDIZED × 2 FE FE (III) ION × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.8
cryo-EM vitrification conditions Cryogen ETHANE-PROPANE
Resolution 1.92 Å
8DBY CryoEM structure of anaerobically prepared nitrogenase MoFe-protein on ultrathin carbon Deposited 2022-06-15 Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 1–523（523 aa）
Chain D 1–523（523 aa）
Not recorded ICS iron-sulfur-molybdenum cluster with interstitial carbon × 2 HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 2 FE FE (III) ION × 2 CLF FE(8)-S(7) CLUSTER × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.8
cryo-EM vitrification conditions Cryogen ETHANE-PROPANE
Resolution 2.26 Å
8DFC CryoEM structure of the 1:1 ADP-tetrafluoroaluminate stabilized nitrogenase complex from Azotobacter vinelandii Deposited 2022-06-21 Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric
Chain B 1–523（523 aa）
Chain D 1–523（523 aa）
Not recorded ICS iron-sulfur-molybdenum cluster with interstitial carbon × 2 HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 2 CLF FE(8)-S(7) CLUSTER × 2 FE FE (III) ION × 2 SF4 IRON/SULFUR CLUSTER × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ALF TETRAFLUOROALUMINATE ION × 2 MG MAGNESIUM ION × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.8
cryo-EM vitrification conditions Cryogen ETHANE-PROPANE
Resolution 2.48 Å
8DFD CryoEM structure of the 2:1 ADP-tetrafluoroaluminate stabilized nitrogenase complex from Azotobacter vinelandii Deposited 2022-06-21 Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric
Chain B 1–523（523 aa）
Chain D 1–523（523 aa）
Not recorded ICS iron-sulfur-molybdenum cluster with interstitial carbon × 2 HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 2 CLF FE(8)-S(7) CLUSTER × 2 FE FE (III) ION × 2 SF4 IRON/SULFUR CLUSTER × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 4 ALF TETRAFLUOROALUMINATE ION × 4 MG MAGNESIUM ION × 4 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.8
cryo-EM vitrification conditions Cryogen ETHANE-PROPANE
Resolution 2.12 Å
8ENL CryoEM structure of the high pH turnover-inactivated nitrogenase MoFe-protein Deposited 2022-09-30 Different construct Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 2–523（522 aa）
Chain D 2–523（522 aa）
Not recorded ICS iron-sulfur-molybdenum cluster with interstitial carbon × 2 UNX UNKNOWN LIGAND × 2 CLF FE(8)-S(7) CLUSTER × 2 1N7 CHAPSO × 2 FE FE (III) ION × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.8
cryo-EM vitrification conditions Cryogen ETHANE-PROPANE
Resolution 2.37 Å
8ENM CryoEM structure of the high pH nitrogenase MoFe-protein under non-turnover conditions Deposited 2022-09-30 Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 1–523（523 aa）
Chain D 1–523（523 aa）
Not recorded ICS iron-sulfur-molybdenum cluster with interstitial carbon × 2 HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 2 CLF FE(8)-S(7) CLUSTER × 2 FE FE (III) ION × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.8
cryo-EM vitrification conditions Cryogen ETHANE-PROPANE
Resolution 2.14 Å
8RHP Cryo-EM structure of the molybdenum nitrogenase complexed with iron protein (NifH) and Shethna protein II (FeSII) Deposited 2023-12-15 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 14 PDB declaration: 14-meric
Chain B 1–523（523 aa）
Chain C 1–523（523 aa）
Chain I 1–523（523 aa）
Chain J 1–523（523 aa）
Not recorded CLF FE(8)-S(7) CLUSTER × 4 HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 4 ICS iron-sulfur-molybdenum cluster with interstitial carbon × 4 CA CALCIUM ION × 4 FES FE2/S2 (INORGANIC) CLUSTER × 2 SF4 IRON/SULFUR CLUSTER × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.89 Å
9CJB CryoEM structure of nitrogenase MoFe-protein 60 minute time point under alkaline turnover Deposited 2024-07-05 Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 1–523（523 aa）
Chain D 1–523（523 aa）
Not recorded ICS iron-sulfur-molybdenum cluster with interstitial carbon × 2 CLF FE(8)-S(7) CLUSTER × 2 FE FE (III) ION × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 9.5
cryo-EM vitrification conditions Cryogen ETHANE-PROPANE
Resolution 1.97 Å
9CJC CryoEM structure of nitrogenase MoFe-protein 20 minute time point under alkaline turnover Deposited 2024-07-05 Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 1–523（523 aa）
Chain D 1–523（523 aa）
Not recorded ICS iron-sulfur-molybdenum cluster with interstitial carbon × 2 HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 1 CLF FE(8)-S(7) CLUSTER × 2 FE FE (III) ION × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 9.5
cryo-EM vitrification conditions Cryogen ETHANE-PROPANE
Resolution 2.04 Å
9CJD CryoEM structure of nitrogenase MoFe-protein 5 minute time point under alkaline turnover Deposited 2024-07-05 Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 1–523（523 aa）
Chain D 1–523（523 aa）
Not recorded ICS iron-sulfur-molybdenum cluster with interstitial carbon × 2 HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 1 CLF FE(8)-S(7) CLUSTER × 2 FE FE (III) ION × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 9.5
cryo-EM vitrification conditions Cryogen ETHANE-PROPANE
Resolution 1.92 Å
9CJE CryoEM structure of nitrogenase MoFe-protein 20 second time point under alkaline turnover Deposited 2024-07-05 Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 1–523（523 aa）
Chain D 1–523（523 aa）
Not recorded ICS iron-sulfur-molybdenum cluster with interstitial carbon × 2 HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 1 CLF FE(8)-S(7) CLUSTER × 2 FE FE (III) ION × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 9.5
cryo-EM vitrification conditions Cryogen ETHANE-PROPANE
Resolution 2.22 Å
9CJF CryoEM structure of alkaline-inactivated nitrogenase MoFe-protein in complex with NafT Deposited 2024-07-05 Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric
Chain B 1–523（523 aa）
Chain D 1–523（523 aa）
Not recorded ICS iron-sulfur-molybdenum cluster with interstitial carbon × 2 CLF FE(8)-S(7) CLUSTER × 2 FE FE (III) ION × 2 1N7 CHAPSO × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.8
cryo-EM vitrification conditions Cryogen ETHANE-PROPANE
Resolution 2.33 Å
9CQX Azotobacter vinelandii Oxidized MoFeP (C1 symmetry) obtained using the SPT Labtech chameleon Deposited 2024-07-19 Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 1–523（523 aa）
Chain D 1–523（523 aa）
Not recorded HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 2 ICS iron-sulfur-molybdenum cluster with interstitial carbon × 2 FE FE (III) ION × 2 CLF FE(8)-S(7) CLUSTER × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE；Samples were frozen with the SPT Labtech chameleon
Resolution 2.51 Å
9CQY Azotobacter vinelandii Oxidized MoFeP (C2 symmetry) obtained using the SPT Labtech chameleon Deposited 2024-07-19 Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 1–523（523 aa）
Chain D 1–523（523 aa）
Not recorded HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 2 ICS iron-sulfur-molybdenum cluster with interstitial carbon × 2 FE FE (III) ION × 2 CLF FE(8)-S(7) CLUSTER × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE；Samples were frozen with the SPT Labtech chameleon
Resolution 2.39 Å
9CQZ Azotobacter vinelandii Reduced MoFeP (C1 symmetry) obtained using the SPT Labtech chameleon of 20 mM sodium dithionite under Al's oil Deposited 2024-07-19 Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 1–523（523 aa）
Chain D 1–523（523 aa）
Not recorded HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 2 ICS iron-sulfur-molybdenum cluster with interstitial carbon × 2 FE FE (III) ION × 2 CLF FE(8)-S(7) CLUSTER × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE；Samples were frozen with the SPT Labtech chameleon
Resolution 2.19 Å
9CR0 Azotobacter vinelandii Reduced MoFeP (C2 symmetry) obtained using the SPT Labtech chameleon of 20 mM sodium dithionite under Al's oil Deposited 2024-07-19 Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 1–523（523 aa）
Chain D 1–523（523 aa）
Not recorded HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 2 ICS iron-sulfur-molybdenum cluster with interstitial carbon × 2 FE FE (III) ION × 2 CLF FE(8)-S(7) CLUSTER × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE；Samples were frozen with the SPT Labtech chameleon
Resolution 2.08 Å
9CTZ Azotobacter vinelandii MoFeP (C2 symmetry) Deposited 2024-07-25 Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 1–523（523 aa）
Chain D 1–523（523 aa）
Not recorded HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 2 ICS iron-sulfur-molybdenum cluster with interstitial carbon × 2 FE FE (III) ION × 2 CLF FE(8)-S(7) CLUSTER × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE；Samples were frozen with the SPT Labtech chameleon
Resolution 2.67 Å
9CU0 Azotobacter vinelandii 1:1:1 MoFeP:FeP:FeSII-Complex (C1 symmetry) Deposited 2024-07-25 Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 7 PDB declaration: heptameric
Chain B 1–523（523 aa）
Chain D 1–523（523 aa）
Not recorded HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 2 ICS iron-sulfur-molybdenum cluster with interstitial carbon × 2 CLF FE(8)-S(7) CLUSTER × 2 FE FE (III) ION × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 2 MG MAGNESIUM ION × 2 SF4 IRON/SULFUR CLUSTER × 1 FES FE2/S2 (INORGANIC) CLUSTER × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE；Samples were frozen with the SPT Labtech chameleon
Resolution 3.94 Å
9CU1 Azotobacter vinelandii filamentous 2:2:1 MoFeP:FeP:FeSII-Complex (termini; C1 symmetry) Deposited 2024-07-25 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 14 PDB declaration: 14-meric
Chain B 1–523（523 aa）
Chain D 1–523（523 aa）
Chain I 1–523（523 aa）
Chain K 1–523（523 aa）
Not recorded HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 4 ICS iron-sulfur-molybdenum cluster with interstitial carbon × 4 CLF FE(8)-S(7) CLUSTER × 4 FE FE (III) ION × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 4 MG MAGNESIUM ION × 4 SF4 IRON/SULFUR CLUSTER × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE；Samples were frozen with the SPT Labtech chameleon
Resolution 2.83 Å
9CU2 Azotobacter vinelandii filamentous 2:2:1 MoFeP:FeP:FeSII-Complex (C2 symmetry) Deposited 2024-07-25 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 14 PDB declaration: 14-meric
Chain B 1–523（523 aa）
Chain D 1–523（523 aa）
Chain I 1–523（523 aa）
Chain K 1–523（523 aa）
Not recorded HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 4 ICS iron-sulfur-molybdenum cluster with interstitial carbon × 4 FE FE (III) ION × 4 CLF FE(8)-S(7) CLUSTER × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 4 MG MAGNESIUM ION × 4 SF4 IRON/SULFUR CLUSTER × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE；Samples were frozen with the SPT Labtech chameleon
Resolution 2.27 Å
9HB9 A. vinelandii nitrogenase MoFe protein Anc1a Deposited 2024-11-05 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 1–523（523 aa）
Chain D 1–523（523 aa）
Not recorded ICS iron-sulfur-molybdenum cluster with interstitial carbon × 2 HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 2 CLF FE(8)-S(7) CLUSTER × 2 MG MAGNESIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；293 K；0.2 M LiSO4 x 1 H2O, 0.1 M bis-Tris/HCl at pH 6.5, 25%(w/v) of polyethylene glycol 3350
Resolution 2.66 Å R-free 0.220
9HBC A. vinelandii nitrogenase MoFe protein Anc2 Deposited 2024-11-06 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 1–523（523 aa）
Chain D 1–523（523 aa）
Not recorded HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 2 ICS iron-sulfur-molybdenum cluster with interstitial carbon × 2 CLF FE(8)-S(7) CLUSTER × 2 TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 1 EDO 1,2-ETHANEDIOL × 2 MG MAGNESIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；293 K；4.5% (w/v) of polyethylene glycol 2000, 3350, 4000 and polyethylene glycol mono methylether 5000, 0.1 M MES/NaOH at pH 6.5, 10% (v/v) of ethylene glycol and 0.15 M Mg acetate
Resolution 1.82 Å R-free 0.225
9MLY Azotobacter vinelandii Reduced MoFeP (C1 symmetry) obtained using the SPT Labtech chameleon of 5 mM sodium dithionite under Al's oil Deposited 2024-12-19 Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 1–523（523 aa）
Chain D 1–523（523 aa）
Not recorded HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 2 ICS iron-sulfur-molybdenum cluster with interstitial carbon × 2 FE FE (III) ION × 2 CLF FE(8)-S(7) CLUSTER × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE；Samples were frozen with the SPT Labtech chameleon
Resolution 2.33 Å
9MLZ Azotobacter vinelandii Reduced MoFeP (C2 symmetry) obtained using the SPT Labtech chameleon of 5 mM sodium dithionite under Al's oil Deposited 2024-12-19 Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 1–523（523 aa）
Chain D 1–523（523 aa）
Not recorded HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 2 ICS iron-sulfur-molybdenum cluster with interstitial carbon × 2 FE FE (III) ION × 2 CLF FE(8)-S(7) CLUSTER × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE；Samples were frozen with the SPT Labtech chameleon
Resolution 2.19 Å
9MM0 Azotobacter vinelandii Reduced MoFeP (C1 symmetry) obtained using the SPT Labtech chameleon of 60 mM sodium dithionite under Al's oil Deposited 2024-12-19 Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 1–523（523 aa）
Chain D 1–523（523 aa）
Not recorded HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 2 ICS iron-sulfur-molybdenum cluster with interstitial carbon × 2 FE FE (III) ION × 2 CLF FE(8)-S(7) CLUSTER × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE；Samples were frozen with the SPT Labtech chameleon
Resolution 2.19 Å
9MM1 Azotobacter vinelandii Reduced MoFeP (C2 symmetry) obtained using the SPT Labtech chameleon of 60 mM sodium dithionite under Al's oil Deposited 2024-12-19 Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 1–523（523 aa）
Chain D 1–523（523 aa）
Not recorded HCA 3-HYDROXY-3-CARBOXY-ADIPIC ACID × 2 ICS iron-sulfur-molybdenum cluster with interstitial carbon × 2 FE FE (III) ION × 2 CLF FE(8)-S(7) CLUSTER × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE；Samples were frozen with the SPT Labtech chameleon
Resolution 2.08 Å

74 other PDB entries and 80 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NIFK_AZOVI
Isoform —
PDB entities 2
Chains and sequence ranges Author chain B； PDBConstruct 1–523； UniProt 1–523 Author chain D； PDBConstruct 1–523； UniProt 1–523 Author chain I； PDBConstruct 1–523； UniProt 1–523 Author chain L； PDBConstruct 1–523； UniProt 1–523

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 8bts

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8bts
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8bts
Deposition date deposition_date2022-11-29
Structure title titleNitrogenase MoFe protein from A. vinelandii alpha double mutant C45A/L158C
Keywords keywordsN2-fixation, Nitrogenase, cooperativity, ammonia, hydrogen, metalloenzyme, FeMo-cofactor, P cluster, O2-sensitivity, OXIDOREDUCTASE; OXIDOREDUCTASE
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier54.81 Å
Radius of gyration Rg (electron density) rg_electron54.59 Å
Forward intensity I(0) i03099500000.00
Molecular weight molecular_weight461680.0 kDa
Excluded volume excluded_volume573650 ų
Envelope volume envelope_volume717890 ų
Hydration-shell volume shell_volume106590 ų
Envelope diameter envelope_diameter184.6 Å
Shell Rg shell_rg60.21 Å
Envelope Rg envelope_rg53.35 Å
Shape Rg shape_rg54.59 Å
Total Rg total_rg54.71 Å
Total atoms total_atoms32158
Residues n_residues3996
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax186.6 Å
Rg (real space) rg_real54.78 Å
Rg uncertainty (real space) rg_real_error1.63 Å
I(0) (real space) i0_real3.1000e+09
I(0) uncertainty (real space) i0_real_error6.4160e+07
Rg (reciprocal space) rg_reciprocal54.82 Å
I(0) (reciprocal space) i0_reciprocal3100000000.0000
Solution quality estimate total_estimate0.8863
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary70.8 Å
Skewness Skewness skewness0.230
Kurtosis Kurtosis kurtosis-0.609
Angular range angular_range— – 0.1450 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha732400000.0000
Real-space data points n_real_points30
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.874; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.896
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (8)

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8. Citations (1)

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9. Files and Curves (10)