2j56

X-ray reduced Paraccocus denitrificans methylamine dehydrogenase N- semiquinone in complex with amicyanin.

Method: X-RAY DIFFRACTION Dmax: 102.6 Å Quality: EXCELLENT

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

AMICYANIN

OrganismNot specified

UniProt P22364

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 27–131 Chain B; UniProt 27–131 Not recorded METHYLAMINE DEHYDROGENASE HEAVY CHAIN × 2 (P29894) METHYLAMINE DEHYDROGENASE LIGHT CHAIN × 2 (P22619) CU COPPER (II) ION × 2 GOL GLYCEROL × 1 NA SODIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 9;pH 9.00 Resolution 2.10 Å R-free 0.207

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.

34 other PDB entries and 57 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name AMCY_PARDE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–105; UniProt 27–131 Author chain B; PDBConstruct 1–105; UniProt 27–131

METHYLAMINE DEHYDROGENASE HEAVY CHAIN

OrganismNot specified

UniProt P29894

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain H; UniProt 32–417 Chain J; UniProt 32–417 Not recorded AMICYANIN × 2 (P22364) METHYLAMINE DEHYDROGENASE LIGHT CHAIN × 2 (P22619) CU COPPER (II) ION × 2 GOL GLYCEROL × 1 NA SODIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 9;pH 9.00 Resolution 2.10 Å R-free 0.207

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.

7 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DHMH_PARDE
Isoform
PDB entities 2
Chains and sequence ranges Author chain H; PDBConstruct 1–386; UniProt 32–417 Author chain J; PDBConstruct 1–386; UniProt 32–417

METHYLAMINE DEHYDROGENASE LIGHT CHAIN

OrganismNot specified

UniProt P22619

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain L; UniProt 58–188 Chain M; UniProt 58–188 Non-standard monomer:Yes (specific site not provided by mmCIF) AMICYANIN × 2 (P22364) METHYLAMINE DEHYDROGENASE HEAVY CHAIN × 2 (P29894) CU COPPER (II) ION × 2 GOL GLYCEROL × 1 NA SODIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 9;pH 9.00 Resolution 2.10 Å R-free 0.207

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.

28 other PDB entries and 37 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DHML_PARDE
Isoform
PDB entities 3
Chains and sequence ranges Author chain L; PDBConstruct 1–131; UniProt 58–188 Author chain M; PDBConstruct 1–131; UniProt 58–188

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 2j56

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2j56
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2j56
Deposition date deposition_date2006-09-12
Structure title titleX-ray reduced Paraccocus denitrificans methylamine dehydrogenase N- semiquinone in complex with amicyanin.
Keywords keywordsOXIDOREDUCTASE, PERIPLASMIC, METAL-BINDING, ELECTRON TRANSPORT, SINGLE CRYSTAL MICROSPECTROPHOTOMETRY; OXIDOREDUCTASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier32.83
Radius of gyration Rg (electron density) rg_electron32.20
Forward intensity I(0) i0284205000.00
Molecular weight molecular_weight133110.0 kDa
Excluded volume excluded_volume165140 ų
Envelope volume envelope_volume199010 ų
Hydration-shell volume shell_volume49734 ų
Envelope diameter envelope_diameter116.1
Shell Rg shell_rg40.51
Envelope Rg envelope_rg32.35
Shape Rg shape_rg32.18
Total Rg total_rg32.85
Total atoms total_atoms9350
Residues n_residues1206
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 dmax102.6
Rg (real space) rg_real32.71
Rg uncertainty (real space) rg_real_error0.60
I(0) (real space) i0_real2.8420e+08
I(0) uncertainty (real space) i0_real_error4.2620e+06
Rg (reciprocal space) rg_reciprocal32.76
I(0) (reciprocal space) i0_reciprocal284200000.0000
Solution quality estimate total_estimate0.9023
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary38.5
Skewness Skewness skewness0.244
Kurtosis Kurtosis kurtosis-0.479
Angular range angular_range— – 0.2400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha63200000.0000
Real-space data points n_real_points49
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.933; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.927

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

7. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (6 domains)

Domain ID domain_idd2j56a_
Class classb — All beta proteins
Fold Fold foldb.6 — Cupredoxin-like
Superfamily Superfamily superfamilyb.6.1 — Cupredoxins
Family Family familyb.6.1.1 — Plastocyanin/azurin-like
Domain ID domain_idd2j56b_
Class classb — All beta proteins
Fold Fold foldb.6 — Cupredoxin-like
Superfamily Superfamily superfamilyb.6.1 — Cupredoxins
Family Family familyb.6.1.1 — Plastocyanin/azurin-like
Domain ID domain_idd2j56h_
Class classb — All beta proteins
Fold Fold foldb.69 — 7-bladed beta-propeller
Superfamily Superfamily superfamilyb.69.2 — YVTN repeat-like/Quinoprotein amine dehydrogenase
Family Family familyb.69.2.0 — automated matches
Domain ID domain_idd2j56j_
Class classb — All beta proteins
Fold Fold foldb.69 — 7-bladed beta-propeller
Superfamily Superfamily superfamilyb.69.2 — YVTN repeat-like/Quinoprotein amine dehydrogenase
Family Family familyb.69.2.0 — automated matches
Domain ID domain_idd2j56l_
Class classg — Small proteins
Fold Fold foldg.21 — Methylamine dehydrogenase, L chain
Superfamily Superfamily superfamilyg.21.1 — Methylamine dehydrogenase, L chain
Family Family familyg.21.1.1 — Methylamine dehydrogenase, L chain
Domain ID domain_idd2j56m_
Class classg — Small proteins
Fold Fold foldg.21 — Methylamine dehydrogenase, L chain
Superfamily Superfamily superfamilyg.21.1 — Methylamine dehydrogenase, L chain
Family Family familyg.21.1.1 — Methylamine dehydrogenase, L chain

CATH v4.4 (6 domains)

Domain ID domain_id2j56A00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily420 — Cupredoxins - blue copper proteins
Domain ID domain_id2j56B00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily420 — Cupredoxins - blue copper proteins
Domain ID domain_id2j56H00
Class class2 — Mainly Beta
Architecture architecture130 — 7 Propeller
Topology topology10 — Methylamine Dehydrogenase; Chain H
Homologous superfamily homologous superfamily10 — YVTN repeat-like/Quinoprotein amine dehydrogenase
Domain ID domain_id2j56J00
Class class2 — Mainly Beta
Architecture architecture130 — 7 Propeller
Topology topology10 — Methylamine Dehydrogenase; Chain H
Homologous superfamily homologous superfamily10 — YVTN repeat-like/Quinoprotein amine dehydrogenase
Domain ID domain_id2j56L00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology30 — Electron Transport Ethylamine Dehydrogenase
Homologous superfamily homologous superfamily10 — Methylamine/Aralkylamine dehydrogenase light chain
Domain ID domain_id2j56M00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology30 — Electron Transport Ethylamine Dehydrogenase
Homologous superfamily homologous superfamily10 — Methylamine/Aralkylamine dehydrogenase light chain

8. Citations (2)

9. Files and Curves (10)