29aj

Crystal Structure of the human mARC1 M187K variant

Method: X-RAY DIFFRACTION Dmax: 77.6 Å Quality: EXCELLENT

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

Mitochondrial amidoxime-reducing component 1,Endolysin

Homo sapiens

UniProt P00720

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain D; UniProt 1–159 Mutation:M187K MTE PHOSPHONIC ACIDMONO-(2-AMINO-5,6-DIMERCAPTO-4-OXO-3,7,8A,9,10,10A-HEXAHYDRO-4H-8-OXA-1,3,9,10-TETRAAZA-ANTHRACEN-7-YLMETHYL)ESTER × 1 B3P 2-[3-(2-HYDROXY-1,1-DIHYDROXYMETHYL-ETHYLAMINO)-PROPYLAMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 1 MOO MOLYBDATE ION × 4 EFK oxidanyl(oxidanylidene)molybdenum × 1 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;291 K;100 mM Bis-TRIS propane, 20 mM Na2MoO4, 10 mM TCEP, 27.5 % PEG3350 Resolution 1.63 Å R-free 0.215

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.

721 other PDB entries and 846 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ENLYS_BPT4
Isoform
PDB entities 1
Chains and sequence ranges Author chain D; PDBConstruct 78–236; UniProt 1–159

Mitochondrial amidoxime-reducing component 1,Endolysin

Homo sapiens

UniProt Q5VT66

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain D; UniProt 53–128 Chain D; UniProt 129–337 Mutation:M187K MTE PHOSPHONIC ACIDMONO-(2-AMINO-5,6-DIMERCAPTO-4-OXO-3,7,8A,9,10,10A-HEXAHYDRO-4H-8-OXA-1,3,9,10-TETRAAZA-ANTHRACEN-7-YLMETHYL)ESTER × 1 B3P 2-[3-(2-HYDROXY-1,1-DIHYDROXYMETHYL-ETHYLAMINO)-PROPYLAMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 1 MOO MOLYBDATE ION × 4 EFK oxidanyl(oxidanylidene)molybdenum × 1 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;291 K;100 mM Bis-TRIS propane, 20 mM Na2MoO4, 10 mM TCEP, 27.5 % PEG3350 Resolution 1.63 Å R-free 0.215

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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MARC1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain D; PDBConstruct 2–77; UniProt 53–128 Author chain D; PDBConstruct 237–445; UniProt 129–337

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 29aj

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 29aj
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2. Structure Basics 2. Structure Basics

Entry ID entry_id29aj
Deposition date deposition_date2026-03-03
最后修订 last_revision2026-03-18
Structure title titleCrystal Structure of the human mARC1 M187K variant
Keywords keywordsenzyme, oxidoreductase, molybdenum, pyranopterin, METAL BINDING PROTEIN; METAL BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier25.26
Radius of gyration Rg (electron density) rg_electron24.18
Forward intensity I(0) i046768500.00
Molecular weight molecular_weight51489.0 kDa
Excluded volume excluded_volume63821 ų
Envelope volume envelope_volume76299 ų
Hydration-shell volume shell_volume26414 ų
Envelope diameter envelope_diameter78.0
Shell Rg shell_rg31.31
Envelope Rg envelope_rg24.21
Shape Rg shape_rg24.14
Total Rg total_rg25.10
Total atoms total_atoms3577
Residues n_residues444
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 dmax77.6
Rg (real space) rg_real25.20
Rg uncertainty (real space) rg_real_error0.45
I(0) (real space) i0_real4.6770e+07
I(0) uncertainty (real space) i0_real_error5.8470e+05
Rg (reciprocal space) rg_reciprocal25.22
I(0) (reciprocal space) i0_reciprocal46770000.0000
Solution quality estimate total_estimate0.9122
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary28.3
Skewness Skewness skewness0.221
Kurtosis Kurtosis kurtosis-0.570
Angular range angular_range— – 0.3150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha13540000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.965; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.966

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)