SAXSdb — 12pb

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

Mitochondrial carrier homolog 2,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	Insufficient information Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 198–217	Mutation：K25E,Y235A,V238D,L199V,A200Y,T226A	UCP1 Nanobody × 1	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

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 12PB	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 mutation/modification 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 mutation/modification 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
8G8W Molecular mechanism of nucleotide inhibition of human uncoupling protein 1 Deposited 2023-02-20	Different construct Different mutation/modification 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 construct Different mutation/modification Different oligomeric state 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	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 construct Different mutation/modification Different oligomeric state 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
8J1N Structure of human UCP1 in the DNP-bound state Deposited 2023-04-13	Different construct Different mutation/modification Different oligomeric state 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	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
9FZQ Proton conductance by human uncoupling protein 1 is inhibited by both purine and pyrimidine nucleotides Deposited 2024-07-05	Different construct Different mutation/modification 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	2
Chains and sequence ranges	Author chain A； PDBConstruct 203–222； UniProt 198–217

Mitochondrial carrier homolog 2,Mitochondrial brown fat uncoupling protein 1

Homo sapiens

UniProt Q9Y6C9

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 Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 1–202 Chain A； UniProt 222–303	Mutation：K25E,Y235A,V238D,L199V,A200Y,T226A	UCP1 Nanobody × 1	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

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 12PB	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 mutation/modification Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–202（202 aa） Chain A 222–303（82 aa）	Mutation：L199V, A200Y, T226A 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 mutation/modification Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–202（202 aa） Chain A 222–303（82 aa）	Mutation：F285N,F286N,L199V,A200Y,T226A 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

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

View Construct and Data Evidence

UniProt name	MTCH2_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain A； PDBConstruct 1–202； UniProt 1–202 Author chain A； PDBConstruct 223–304； UniProt 222–303

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	12pb
Deposition date deposition_date	2026-04-14
Structure title title	Single particle cryo-EM structure of human MTCH2 (hyperactive mutant K25E Y235A V238D)
Keywords keywords	mitochondrial outer membrane insertase, SLC25 carrier fold, hydrophilic groove, membrane protein biogenesis, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method method	ELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier	29.40 Å
Radius of gyration Rg (electron density) rg_electron	28.96 Å
Forward intensity I(0) i0	32792100.00
Molecular weight molecular_weight	45077.0 kDa
Excluded volume excluded_volume	56739 Å³
Envelope volume envelope_volume	76098 Å³
Hydration-shell volume shell_volume	23834 Å³
Envelope diameter envelope_diameter	98.2 Å
Shell Rg shell_rg	33.68 Å
Envelope Rg envelope_rg	28.11 Å
Shape Rg shape_rg	28.95 Å
Total Rg total_rg	29.55 Å
Total atoms total_atoms	3168
Residues n_residues	410
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

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

Maximum dimension Dmax dmax	97.1 Å
Rg (real space) rg_real	29.61 Å
Rg uncertainty (real space) rg_real_error	0.82 Å
I(0) (real space) i0_real	3.2790e+07
I(0) uncertainty (real space) i0_real_error	4.9840e+05
Rg (reciprocal space) rg_reciprocal	29.52 Å
I(0) (reciprocal space) i0_reciprocal	32790000.0000
Solution quality estimate total_estimate	0.8492
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	25.2 Å
Skewness Skewness skewness	0.413
Kurtosis Kurtosis kurtosis	-0.666
Angular range angular_range	— – 0.2700 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	3332000.0000
Real-space data points n_real_points	55
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.802; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.743; Smooth: 0.886

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Description description	UCP1 Nanobody
Molecular weight formula_weight	13913.5 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B
Atom count atom_count	3180

GQRQLVESGGGLVQPGGSLRLSCAASGRTSSTYTMGWFRQAPGKEREFVAAISWTGTPYYADSVKGRFTISRDNAKNTVYLQMNSLEPEDTAVYYCAAARPGLFIFVSDYARTAKYDYWGKGTPVTV

来源 Source

来源生物 organism	synthetic construct
NCBI Class编号 ncbi_taxonomy_id	32630
宿主生物 host_organism	Escherichia coli BL21(DE3)

Entity 2 Entity 2 polymer

Description description	Mitochondrial carrier homolog 2,Mitochondrial brown fat uncoupling protein 1
Molecular weight formula_weight	33481.0 kDa
Mutation mutation	K25E,Y235A,V238D,L199V,A200Y,T226A
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A

MADAASQVLLGSGLTILSQPLMYVEVLIQVGYEPLPPTIGRNIFGRQVCQLPGLFSYAQHIASIDGRRGLFTGLTPRLCSGVLGTVVHGKVLQHYQESDKGEELGPGNVQKEVSSSFDHVIKETTREMIARSAATLITHPFHVITLRSMVQFIGRESKYCGLCDSIITIYREEGILGFFAGLVPRLLGDILSLWLCNSVYYLMKEAFVKNNILADDVPCHLVSQAVAGFFASMLTAPFDLVSNLMAVNNCGLAGGCPPYSPIYTSWIDCWCMLQKEGNMSRGNSLFFRKVPFGKTYCCDLKMLI

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	Spodoptera frugiperda

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8. Citations (1)

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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	3.100 Å
Low-resolution limit resolution_low	— Å
R factor r_factor	—
R_work r_work	—
R_free r_free	—

Resolution resolution	3.10 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	612877

fit	/app/data/saxs_computation/2p/12pb/12pb.fit
pddf	/app/data/pr_computation/2p/12pb/12pb.pr.out
profile	/app/data/saxs_computation/2p/12pb/12pb.dat

Single particle cryo-EM structure of human MTCH2 (hyperactive mutant K25E Y235A V238D)

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

Mitochondrial carrier homolog 2,Mitochondrial brown fat uncoupling protein 1

State in the Current Structure

Other States of the Same Protein in the Database

Mitochondrial carrier homolog 2,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

Refinement Refinement

冷冻电镜 EM 3D

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)