6wti

The Cryo-EM structure of the ubiquinol oxidase from Escherichia coli

Method: ELECTRON MICROSCOPY D_max: 102.4 Å Quality: EXCELLENT

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

Cytochrome o ubiquinol oxidase, subunit I

Escherichia coli

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 1–663	Not recorded	Ubiquinol oxidase subunit 2 × 1 （A0A024L5V9） Cytochrome o ubiquinol oxidase × 1 （D6I7E4） Cytochrome o ubiquinol oxidase, subunit IV × 1 （I2RK84） HEM PROTOPORPHYRIN IX CONTAINING FE × 1 HEO HEME O × 1 CU COPPER (II) ION × 1 UQ8 Ubiquinone-8 × 1 3PE 1,2-Distearoyl-sn-glycerophosphoethanolamine × 9 U9V pentadecyl(tetradecyl)peroxyanhydride × 1	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 2.38 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 6WTI	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
7N9Z E. coli cytochrome bo3 in MSP nanodisc Deposited 2021-06-19	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain F 1–663（663 aa）	Not recorded	UQ8 Ubiquinone-8 × 1 LHG 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE × 9 3PE 1,2-Distearoyl-sn-glycerophosphoethanolamine × 2 HEO HEME O × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 1 CDL CARDIOLIPIN × 1 CU COPPER (II) ION × 1 ZN ZINC ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.19 Å

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	H4KCU1_ECOLX
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–663； UniProt 1–663

Ubiquinol oxidase subunit 2

Escherichia coli

UniProt A0A024L5V9

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 1–315	Not recorded	Cytochrome o ubiquinol oxidase, subunit I × 1 （H4KCU1） Cytochrome o ubiquinol oxidase × 1 （D6I7E4） Cytochrome o ubiquinol oxidase, subunit IV × 1 （I2RK84） HEM PROTOPORPHYRIN IX CONTAINING FE × 1 HEO HEME O × 1 CU COPPER (II) ION × 1 UQ8 Ubiquinone-8 × 1 3PE 1,2-Distearoyl-sn-glycerophosphoethanolamine × 9 U9V pentadecyl(tetradecyl)peroxyanhydride × 1	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 2.38 Å

Other States of the Same Protein in the Database

Other PDB	Difference from Current Entry 6WTI	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
7N9Z E. coli cytochrome bo3 in MSP nanodisc Deposited 2021-06-19	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain G 1–315（315 aa）	Not recorded	UQ8 Ubiquinone-8 × 1 LHG 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE × 9 3PE 1,2-Distearoyl-sn-glycerophosphoethanolamine × 2 HEO HEME O × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 1 CDL CARDIOLIPIN × 1 CU COPPER (II) ION × 1 ZN ZINC ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.19 Å
7XMC Cryo-EM structure of Cytochrome bo3 from Escherichia coli, apo structure with DMSO Deposited 2022-04-25	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 1–315（315 aa）	Not recorded	HEO HEME O × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 1 CU COPPER (II) ION × 1 PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 2 UNX UNKNOWN LIGAND × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.09 Å
7XMD Cryo-EM structure of Cytochrome bo3 from Escherichia coli, the structure complexed with an allosteric inhibitor N4 Deposited 2022-04-25	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 1–315（315 aa）	Not recorded	HEO HEME O × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 1 CU COPPER (II) ION × 1 PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 2 JYR methyl 3-oxidanyl-5-[oxidanyl(oxidanylidene)-$l^{4}-azanyl]-1-benzothiophene-2-carboxylate × 1 UNX UNKNOWN LIGAND × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.2 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.99 Å

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	A0A024L5V9_ECOLX
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–315； UniProt 1–315

Cytochrome o ubiquinol oxidase

Escherichia coli

UniProt D6I7E4

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 C； UniProt 1–204	Not recorded	Cytochrome o ubiquinol oxidase, subunit I × 1 （H4KCU1） Ubiquinol oxidase subunit 2 × 1 （A0A024L5V9） Cytochrome o ubiquinol oxidase, subunit IV × 1 （I2RK84） HEM PROTOPORPHYRIN IX CONTAINING FE × 1 HEO HEME O × 1 CU COPPER (II) ION × 1 UQ8 Ubiquinone-8 × 1 3PE 1,2-Distearoyl-sn-glycerophosphoethanolamine × 9 U9V pentadecyl(tetradecyl)peroxyanhydride × 1	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 2.38 Å

Other States of the Same Protein in the Database

Other PDB	Difference from Current Entry 6WTI	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
7N9Z E. coli cytochrome bo3 in MSP nanodisc Deposited 2021-06-19	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain H 1–204（204 aa）	Not recorded	UQ8 Ubiquinone-8 × 1 LHG 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE × 9 3PE 1,2-Distearoyl-sn-glycerophosphoethanolamine × 2 HEO HEME O × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 1 CDL CARDIOLIPIN × 1 CU COPPER (II) ION × 1 ZN ZINC ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.19 Å

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	D6I7E4_ECOLX
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain C； PDBConstruct 1–204； UniProt 1–204

Cytochrome o ubiquinol oxidase, subunit IV

Escherichia coli

UniProt I2RK84

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 D； UniProt 1–109	Not recorded	Cytochrome o ubiquinol oxidase, subunit I × 1 （H4KCU1） Ubiquinol oxidase subunit 2 × 1 （A0A024L5V9） Cytochrome o ubiquinol oxidase × 1 （D6I7E4） HEM PROTOPORPHYRIN IX CONTAINING FE × 1 HEO HEME O × 1 CU COPPER (II) ION × 1 UQ8 Ubiquinone-8 × 1 3PE 1,2-Distearoyl-sn-glycerophosphoethanolamine × 9 U9V pentadecyl(tetradecyl)peroxyanhydride × 1	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 2.38 Å

Other States of the Same Protein in the Database

Other PDB	Difference from Current Entry 6WTI	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
7N9Z E. coli cytochrome bo3 in MSP nanodisc Deposited 2021-06-19	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain I 1–109（109 aa）	Not recorded	UQ8 Ubiquinone-8 × 1 LHG 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE × 9 3PE 1,2-Distearoyl-sn-glycerophosphoethanolamine × 2 HEO HEME O × 1 HEM PROTOPORPHYRIN IX CONTAINING FE × 1 CDL CARDIOLIPIN × 1 CU COPPER (II) ION × 1 ZN ZINC ION × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.19 Å

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	I2RK84_ECOLX
Isoform	—
PDB entities	4
Chains and sequence ranges	Author chain D； PDBConstruct 1–109； UniProt 1–109

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

P(r) Distance Distribution P(r) Distribution

Download Download SAXS (.dat) P(r) (.pr.out) CIF

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	6wti
Deposition date deposition_date	2020-05-02
Structure title title	The Cryo-EM structure of the ubiquinol oxidase from Escherichia coli
Keywords keywords	ubiquinol oxidase cytochrome bo3, membrane protein, OXIDOREDUCTASE; OXIDOREDUCTASE
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	33.02 Å
Radius of gyration Rg (electron density) rg_electron	31.52 Å
Forward intensity I(0) i0	241066000.00
Molecular weight molecular_weight	141460.0 kDa
Excluded volume excluded_volume	183740 Å³
Envelope volume envelope_volume	213560 Å³
Hydration-shell volume shell_volume	53558 Å³
Envelope diameter envelope_diameter	111.0 Å
Shell Rg shell_rg	40.56 Å
Envelope Rg envelope_rg	31.88 Å
Shape Rg shape_rg	31.52 Å
Total Rg total_rg	32.31 Å
Total atoms total_atoms	9980
Residues n_residues	1207
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	102.4 Å
Rg (real space) rg_real	32.84 Å
Rg uncertainty (real space) rg_real_error	0.61 Å
I(0) (real space) i0_real	2.4110e+08
I(0) uncertainty (real space) i0_real_error	3.5580e+06
Rg (reciprocal space) rg_reciprocal	32.92 Å
I(0) (reciprocal space) i0_reciprocal	241100000.0000
Solution quality estimate total_estimate	0.9005
Solution quality rating solution_quality	EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	40.5 Å
Skewness Skewness skewness	0.200
Kurtosis Kurtosis kurtosis	-0.454
Angular range angular_range	— – 0.2400 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	51680000.0000
Real-space data points n_real_points	49
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.933; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.991; Smooth: 0.913

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (10)

Entity 1 Entity 1 polymer

Description description	Cytochrome o ubiquinol oxidase, subunit I
Molecular weight formula_weight	74424.5 kDa
EC 编号 ec_number	1.10.3.-
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	9980

MFGKLSLDAVPFHEPIVMVTIAGIILGGLALVGLITYFGKWTYLWKEWLTSVDHKRLGIMYIIVAIVMLLRGFADAIMMRSQQALASAGEAGFLPPHHYDQIFTAHGVIMIFFVAMPFVIGLMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFSRKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQQIDPQFHTMLMIAASGAVLIALGILCLVIQMYVSIRDRDQNRDLTGDPWGGRTLEWATSSPPPFYNFAVVPHVHERDAFWEMKEKGEAYKKPDHYEEIHMPKNSGAGIVIAAFSTIFGFAMIWHIWWLAIVGFAGMIITWIVKSFDEDVDYYVPVAEIEKLENQHFDEITKAGLKNGN

来源 Source

来源生物 organism	Escherichia coli
NCBI Class编号 ncbi_taxonomy_id	562
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	Ubiquinol oxidase subunit 2
Molecular weight formula_weight	34947.2 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B

MRLRKYNKSLGWLSLFAGTVLLSGCNSALLDPKGQIGLEQRSLILTAFGLMLIVVIPAILMAVGFAWKYRASNKDAKYSPNWSHSNKVEAVVWTVPILIIIFLAVLTWKTTHALEPSKPLAHDEKPITIEVVSMDWKWFFIYPEQGIATVNEIAFPANTPVYFKVTSNSVMNSFFIPRLGSQIYAMAGMQTRLHLIANEPGTYDGISASYSGPGFSGMKFKAIATPDRAAFDQWVAKAKQSPNTMSDMAAFEKLAAPSEYNQVEYFSNVKPDLFADVINKFMAHGKSMDMTQPEGEHSAHEGMEGMDMSHAESAH

来源 Source

来源生物 organism	Escherichia coli
NCBI Class编号 ncbi_taxonomy_id	562
宿主生物 host_organism	Escherichia coli

Entity 3 Entity 3 polymer

Description description	Cytochrome o ubiquinol oxidase
Molecular weight formula_weight	22642.6 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C

MATDTLTHATAHAHEHGHHDAGGTKIFGFWIYLMSDCILFSILFATYAVLVNGTAGGPTGKDIFELPFVLVETFLLLFSSITYGMAAIAMYKNNKSQVISWLALTWLFGAGFIGMEIYEFHHLIVNGMGPDRSGFLSAFFALVGTHGLHVTSGLIWMAVLMVQIARRGLTSTNRTRIMCLSLFWHFLDVVWICVFTVVYLMGAM

来源 Source

来源生物 organism	Escherichia coli
NCBI Class编号 ncbi_taxonomy_id	562
宿主生物 host_organism	Escherichia coli

Entity 4 Entity 4 polymer

Description description	Cytochrome o ubiquinol oxidase, subunit IV
Molecular weight formula_weight	12037.4 kDa
EC 编号 ec_number	1.10.3.-
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	D

MSHSTDHSGASHGSVKTYMTGFILSIILTVIPFWMVMTGAASPAVILGTILAMAVVQVLVHLVCFLHMNTKSDEGWNMTAFVFTVLIIAILVVGSIWIMWNLNYNMMMH

来源 Source

来源生物 organism	Escherichia coli
NCBI Class编号 ncbi_taxonomy_id	562
宿主生物 host_organism	Escherichia coli

Entity 5 Entity 5 non-polymer

Description description	PROTOPORPHYRIN IX CONTAINING FE
Molecular weight formula_weight	616.5 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 6 Entity 6 non-polymer

Description description	HEME O
Molecular weight formula_weight	838.9 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 7 Entity 7 non-polymer

Description description	COPPER (II) ION
Molecular weight formula_weight	63.5 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 8 Entity 8 non-polymer

Description description	Ubiquinone-8
Molecular weight formula_weight	727.1 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 9 Entity 9 non-polymer

Description description	1,2-Distearoyl-sn-glycerophosphoethanolamine
Molecular weight formula_weight	748.1 kDa
Source method src_method	syn
Copy count entity_count	9

Entity 10 Entity 10 non-polymer

Description description	pentadecyl(tetradecyl)peroxyanhydride
Molecular weight formula_weight	524.9 kDa
Source method src_method	syn
Copy count entity_count	1

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d6wtib1
Class class	f — Membrane and cell surface proteins and peptides
Fold Fold fold	f.17 — Transmembrane helix hairpin
Superfamily Superfamily superfamily	f.17.2 — Cytochrome c oxidase subunit II-like, transmembrane region
Family Family family	f.17.2.1 — Cytochrome c oxidase subunit II-like, transmembrane region

Domain ID domain_id	d6wtib2
Class class	b — All beta proteins
Fold Fold fold	b.6 — Cupredoxin-like
Superfamily Superfamily superfamily	b.6.1 — Cupredoxins
Family Family family	b.6.1.2 — Periplasmic domain of cytochrome c oxidase subunit II

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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	2.38 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	334222

fit	/app/data/saxs_computation/wt/6wti/6wti.fit
pddf	/app/data/pr_computation/wt/6wti/6wti.pr.out
profile	/app/data/saxs_computation/wt/6wti/6wti.dat

The Cryo-EM structure of the ubiquinol oxidase from Escherichia coli

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

Cytochrome o ubiquinol oxidase, subunit I

State in the Current Structure

Other States of the Same Protein in the Database

Ubiquinol oxidase subunit 2

State in the Current Structure

Other States of the Same Protein in the Database

Cytochrome o ubiquinol oxidase

State in the Current Structure

Other States of the Same Protein in the Database

Cytochrome o ubiquinol oxidase, subunit IV

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 (10)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

Entity 3 Entity 3 polymer

Polymer Polymer

来源 Source

Entity 4 Entity 4 polymer

Polymer Polymer

来源 Source

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 non-polymer

Entity 7 Entity 7 non-polymer

Entity 8 Entity 8 non-polymer

Entity 9 Entity 9 non-polymer

Entity 10 Entity 10 non-polymer

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (2 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)