9cje

CryoEM structure of nitrogenase MoFe-protein 20 second time point under alkaline turnover

Method: ELECTRON MICROSCOPY Dmax: 119.5 Å Quality: GOOD

1. Protein Identity and Related Structures Protein Identity & Related Structures

Nitrogenase molybdenum-iron protein alpha chain

OrganismNot specified

UniProt P07328

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 1–492 Chain C; UniProt 1–492 Not recorded Nitrogenase molybdenum-iron protein beta chain × 2 (P07329) 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

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.

83 other PDB entries and 89 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NIFD_AZOVI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–492; UniProt 1–492 Author chain C; PDBConstruct 1–492; UniProt 1–492

Nitrogenase molybdenum-iron protein beta chain

OrganismNot specified

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 molybdenum-iron protein alpha chain × 2 (P07328) 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

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.

74 other PDB entries and 81 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

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 9cje

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9cje
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9cje
Deposition date deposition_date2024-07-05
Structure title titleCryoEM structure of nitrogenase MoFe-protein 20 second time point under alkaline turnover
Keywords keywordsOxidoreductase, METAL BINDING PROTEIN; METAL BINDING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier37.53
Radius of gyration Rg (electron density) rg_electron36.92
Forward intensity I(0) i0726533000.00
Molecular weight molecular_weight218940.0 kDa
Excluded volume excluded_volume272440 ų
Envelope volume envelope_volume310740 ų
Hydration-shell volume shell_volume66993 ų
Envelope diameter envelope_diameter122.2
Shell Rg shell_rg45.27
Envelope Rg envelope_rg36.94
Shape Rg shape_rg36.92
Total Rg total_rg37.36
Total atoms total_atoms15256
Residues n_residues1906
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −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

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax119.5
Rg (real space) rg_real37.40
Rg uncertainty (real space) rg_real_error0.60
I(0) (real space) i0_real7.2650e+08
I(0) uncertainty (real space) i0_real_error1.1810e+07
Rg (reciprocal space) rg_reciprocal37.48
I(0) (reciprocal space) i0_reciprocal726600000.0000
Solution quality estimate total_estimate0.8975
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary42.7
Skewness Skewness skewness0.239
Kurtosis Kurtosis kurtosis-0.537
Angular range angular_range— – 0.2100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha188600000.0000
Real-space data points n_real_points43
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.919; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.994; Smooth: 0.913

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)