6o7q

Nitrogenase MoFeP mutant S188A from Azotobacter vinelandii in the dithionite reduced state after redox cycling

Method: X-RAY DIFFRACTION Dmax: 122.3 Å Quality: REASONABLE

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) 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

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 Mutation:S188A Nitrogenase molybdenum-iron protein alpha chain × 2 (P07328) 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

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 6o7q

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6o7q
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6o7q
Deposition date deposition_date2019-03-08
Structure title titleNitrogenase MoFeP mutant S188A from Azotobacter vinelandii in the dithionite reduced state after redox cycling
Keywords keywordsNitrogenase, S188A, MoFeP, OXIDOREDUCTASE; OXIDOREDUCTASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier38.27
Radius of gyration Rg (electron density) rg_electron37.65
Forward intensity I(0) i0784990000.00
Molecular weight molecular_weight227550.0 kDa
Excluded volume excluded_volume282910 ų
Envelope volume envelope_volume327890 ų
Hydration-shell volume shell_volume69161 ų
Envelope diameter envelope_diameter123.1
Shell Rg shell_rg46.11
Envelope Rg envelope_rg37.68
Shape Rg shape_rg37.65
Total Rg total_rg38.04
Total atoms total_atoms31216
Residues n_residues1992
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 dmax122.3
Rg (real space) rg_real38.16
Rg uncertainty (real space) rg_real_error0.71
I(0) (real space) i0_real7.8500e+08
I(0) uncertainty (real space) i0_real_error1.3080e+07
Rg (reciprocal space) rg_reciprocal38.23
I(0) (reciprocal space) i0_reciprocal785000000.0000
Solution quality estimate total_estimate0.6973
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary44.8
Skewness Skewness skewness0.249
Kurtosis Kurtosis kurtosis-0.551
Angular range angular_range— – 0.2050 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha257100000.0000
Real-space data points n_real_points42
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.914; Stabil: 1.000; Sysdev: 0.132; Positv: 1.000; Valcen: 0.997; Smooth: 0.926

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

7. Fold Classification (SCOP + CATH) 18 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd6o7qa_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.92 — Chelatase-like
Superfamily Superfamily superfamilyc.92.2 — 'Helical backbone' metal receptor
Family Family familyc.92.2.3 — Nitrogenase iron-molybdenum protein
Domain ID domain_idd6o7qb_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.92 — Chelatase-like
Superfamily Superfamily superfamilyc.92.2 — 'Helical backbone' metal receptor
Family Family familyc.92.2.3 — Nitrogenase iron-molybdenum protein
Domain ID domain_idd6o7qc_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.92 — Chelatase-like
Superfamily Superfamily superfamilyc.92.2 — 'Helical backbone' metal receptor
Family Family familyc.92.2.3 — Nitrogenase iron-molybdenum protein
Domain ID domain_idd6o7qd_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.92 — Chelatase-like
Superfamily Superfamily superfamilyc.92.2 — 'Helical backbone' metal receptor
Family Family familyc.92.2.3 — Nitrogenase iron-molybdenum protein

CATH v4.4 (14 domains)

Domain ID domain_id6o7qA01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily1980 — Nitrogenase molybdenum iron protein domain
Domain ID domain_id6o7qA02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily1980 — Nitrogenase molybdenum iron protein domain
Domain ID domain_id6o7qA03
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily1980 — Nitrogenase molybdenum iron protein domain
Domain ID domain_id6o7qB01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily1980 — Nitrogenase molybdenum iron protein domain
Domain ID domain_id6o7qB02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily1980 — Nitrogenase molybdenum iron protein domain
Domain ID domain_id6o7qB03
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology89 — Nitrogenase Molybdenum-iron Protein, subunit B; domain 4
Homologous superfamily homologous superfamily10 — Nitrogenase Molybdenum-iron Protein, subunit B, domain 4
Domain ID domain_id6o7qB04
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily1980 — Nitrogenase molybdenum iron protein domain
Domain ID domain_id6o7qC01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily1980 — Nitrogenase molybdenum iron protein domain
Domain ID domain_id6o7qC02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily1980 — Nitrogenase molybdenum iron protein domain
Domain ID domain_id6o7qC03
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily1980 — Nitrogenase molybdenum iron protein domain
Domain ID domain_id6o7qD01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily1980 — Nitrogenase molybdenum iron protein domain
Domain ID domain_id6o7qD02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily1980 — Nitrogenase molybdenum iron protein domain
Domain ID domain_id6o7qD03
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology89 — Nitrogenase Molybdenum-iron Protein, subunit B; domain 4
Homologous superfamily homologous superfamily10 — Nitrogenase Molybdenum-iron Protein, subunit B, domain 4
Domain ID domain_id6o7qD04
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily1980 — Nitrogenase molybdenum iron protein domain

8. Citations (1)

9. Files and Curves (10)