SAXSdb — 8j1n

▼

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

Mitochondrial brown fat uncoupling protein 1

Homo sapiens

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 × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 1–307	Not recorded	Sybody 12F2 × 1 DNF 2,4-DINITROPHENOL × 1 CDL CARDIOLIPIN × 1 PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 2	ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 2.51 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.

Other PDB	Difference from Current Entry 8J1N	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
12OY Single particle cryo-EM structure of human MTCH2 Deposited 2026-04-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 198–217（20 aa）	Mutation：L199V, A200Y, T226A	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5；50 mM HEPES/KOH pH 7.5, 200 mM NaCl, 2 mM Mg Acetate, and 0.07% UDM cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.60 Å
12OZ Single particle cryo-EM structure of human MTCH2 (hyperactive mutant F285N F286N) Deposited 2026-04-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 198–217（20 aa）	Mutation：F285N,F286N,L199V,A200Y,T226A	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5；50 mM HEPES/KOH pH 7.5, 200 mM NaCl, 2 mM Mg Acetate, and 0.07% UDM cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.30 Å
12PB Single particle cryo-EM structure of human MTCH2 (hyperactive mutant K25E Y235A V238D) Deposited 2026-04-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 198–217（20 aa）	Mutation：K25E,Y235A,V238D,L199V,A200Y,T226A	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5；50 mM HEPES/KOH pH 7.5, 200 mM NaCl, 2 mM Mg Acetate, and 0.07% UDM cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.10 Å
8G8W Molecular mechanism of nucleotide inhibition of human uncoupling protein 1 Deposited 2023-02-20	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 2–307（306 aa）	Not recorded	GTP GUANOSINE-5'-TRIPHOSPHATE × 1 CDL CARDIOLIPIN × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 6 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.80 Å
8HBV Structure of human UCP1 in the nucleotide-free state Deposited 2022-10-31	Different ligand/ion Different experimental conditions	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–307（307 aa）	Not recorded	CDL CARDIOLIPIN × 1 PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.51 Å
8HBW Structure of human UCP1 in the ATP-bound state Deposited 2022-10-31	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–307（307 aa）	Not recorded	ATP ADENOSINE-5'-TRIPHOSPHATE × 1 CDL CARDIOLIPIN × 1 PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.57 Å
9FZQ Proton conductance by human uncoupling protein 1 is inhibited by both purine and pyrimidine nucleotides Deposited 2024-07-05	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 2–307（306 aa）	Not recorded	UTP URIDINE 5'-TRIPHOSPHATE × 1 CDL CARDIOLIPIN × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 6 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.03 Å

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

View Construct and Data Evidence

UniProt name	UCP1_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 57–363； UniProt 1–307

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.

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id	8j1n
Deposition date deposition_date	2023-04-13
Structure title title	Structure of human UCP1 in the DNP-bound state
Keywords keywords	UCP1, SLC25A7, thermogenin, SLC25, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method method	ELECTRON MICROSCOPY

▼

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

Radius of gyration Rg (Guinier) rg_guinier	26.12 Å
Radius of gyration Rg (electron density) rg_electron	25.82 Å
Forward intensity I(0) i0	35372700.00
Molecular weight molecular_weight	46856.0 kDa
Excluded volume excluded_volume	59031 Å³
Envelope volume envelope_volume	70667 Å³
Hydration-shell volume shell_volume	24609 Å³
Envelope diameter envelope_diameter	103.3 Å
Shell Rg shell_rg	31.05 Å
Envelope Rg envelope_rg	26.37 Å
Shape Rg shape_rg	25.84 Å
Total Rg total_rg	26.37 Å
Total atoms total_atoms	3292
Residues n_residues	414
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

▼

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

Maximum dimension Dmax dmax	98.2 Å
Rg (real space) rg_real	26.41 Å
Rg uncertainty (real space) rg_real_error	1.02 Å
I(0) (real space) i0_real	3.5370e+07
I(0) uncertainty (real space) i0_real_error	5.1250e+05
Rg (reciprocal space) rg_reciprocal	26.32 Å
I(0) (reciprocal space) i0_reciprocal	35370000.0000
Solution quality estimate total_estimate	0.7901
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	25.8 Å
Skewness Skewness skewness	0.664
Kurtosis Kurtosis kurtosis	0.133
Angular range angular_range	— – 0.3050 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	4787000.0000
Real-space data points n_real_points	62
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.560; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.591; Smooth: 0.996

▶

5. Crystallography and Experiment 5. Crystallography & Experiment

▶

6. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Description description	Mitochondrial brown fat uncoupling protein 1
Molecular weight formula_weight	39468.4 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	3292

MSRLEEELRRRLTEGSGGWSHPQFEKGSGDYKDDDDKGSGWSHPQFEKLEVLFQGPMGGLTASDVHPTLGVQLFSAGIAACLADVITFPLDTAKVRLQVQGECPTSSVIRYKGVLGTITAVVKTEGRMKLYSGLPAGLQRQISSASLRIGLYDTVQEFLTAGKETAPSLGSKILAGLTTGGVAVFIGQPTEVVKVRLQAQSHLHGIKPRYTGTYNAYRIIATTEGLTGLWKGTTPNLMRSVIINCTELVTYDLMKEAFVKNNILADDVPCHLVSALIAGFCATAMSSPVDVVKTRFINSPPGQYKSVPNCAMKVFTNEGPTAFFKGLVPSFLRLGSWNVIMFVCFEQLKRELSKSRQTMDCAT

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Homo sapiens

Entity 2 Entity 2 polymer

Description description	Sybody 12F2
Molecular weight formula_weight	15004.7 kDa
Source method src_method	syn
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B

MGQVQLVESGGGLVQAGGSLRLSCAASGFPVMYYNMHWYRQAPGKEREWVAAIESTGWWAHYADSVKGRFTISRDNAKNTVYLQMNSLKPEDTAVYYCNVKDFGWRWEAYDYWGQGTQVTVSSLEHHHHHH

Entity 3 Entity 3 non-polymer

Description description	2,4-DINITROPHENOL
Molecular weight formula_weight	184.1 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 4 Entity 4 non-polymer

Description description	CARDIOLIPIN
Molecular weight formula_weight	1464.0 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 5 Entity 5 non-polymer

Description description	1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE
Molecular weight formula_weight	790.1 kDa
Source method src_method	syn
Copy count entity_count	2

▼

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id	8j1nB01
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

▶

8. Citations (1)

▶

Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	—

Space group space_group	P 1
Space-group number int_tables_number	1
Crystal system crystal_system	—

Resolution resolution	2.51 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	709625

fit	/app/data/saxs_computation/j1/8j1n/8j1n.fit
pddf	/app/data/pr_computation/j1/8j1n/8j1n.pr.out
profile	/app/data/saxs_computation/j1/8j1n/8j1n.dat

Structure of human UCP1 in the DNP-bound state

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

Mitochondrial brown fat uncoupling protein 1

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

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

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

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

冷冻电镜 EM 3D

6. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 non-polymer

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)