SAXSdb — 1d5f

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

E6AP HECT CATALYTIC DOMAIN, E3 LIGASE

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 homooligomer Homooligomer Protein × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain A； UniProt 495–852 Chain B； UniProt 495–852 Chain C； UniProt 495–852	Not recorded	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；PEG1500, AMMONIUM ACETATE,SODIUM CHLORIDE, HEPES-NA, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 277.0K	Resolution 2.80 Å R-free 0.283

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 1D5F	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1C4Z STRUCTURE OF AN E6AP-UBCH7 COMPLEX: INSIGHTS INTO THE UBIQUITINATION PATHWAY Deposited 1999-10-14	Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 518–875（358 aa） Fragment：HECT CATALYTIC DOMAIN Chain B 518–875（358 aa） Fragment：HECT CATALYTIC DOMAIN Chain C 518–875（358 aa） Fragment：HECT CATALYTIC DOMAIN	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；PEG1500, MAGNESIUM CHLORIDE, MES-NA, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 277.0K	Resolution 2.60 Å R-free 0.290
1EQX SOLUTION STRUCTURE DETERMINATION AND MUTATIONAL ANALYSIS OF THE PAPILLOMAVIRUS E6-INTERACTING PEPTIDE OF E6AP Deposited 2000-04-06	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 401–418（18 aa） Fragment：E6-INTERACTING PEPTIDE	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.2；288 K；Ionic strength (raw mmCIF value) 10 mM Na3PO4；Pressure ambient NMR sample composition 2 mM E6ap; 10 mM phosphate buffer; 40% TFE, 60% H2O \| 40% TFE, 60% H2O	Resolution not provided
4GIZ Crystal structure of full-length human papillomavirus oncoprotein E6 in complex with LXXLL peptide of ubiquitin ligase E6AP at 2.55 A resolution Deposited 2012-08-09	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 403–414（12 aa） Fragment：unp residues 27-392/403-414	Mutation：D83A,K84A,K240A,E360A,D364A,K363A	ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 9.5；290 K；10% peg8000, pH 9.5, VAPOR DIFFUSION, SITTING DROP, temperature 290K	Resolution 2.55 Å R-free 0.196
4GIZ Crystal structure of full-length human papillomavirus oncoprotein E6 in complex with LXXLL peptide of ubiquitin ligase E6AP at 2.55 A resolution Deposited 2012-08-09	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 403–414（12 aa） Fragment：unp residues 27-392/403-414	Mutation：D83A,K84A,K240A,E360A,D364A,K363A	ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 9.5；290 K；10% peg8000, pH 9.5, VAPOR DIFFUSION, SITTING DROP, temperature 290K	Resolution 2.55 Å R-free 0.196
6SJV Structure of HPV18 E6 oncoprotein in complex with mutant E6AP LxxLL motif Deposited 2019-08-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 403–417（15 aa）	Mutation：;K84A,K240A,E360A,K363A,D364A,F1049R,L2386F,E2393R,K84A,K240A,E360A,K363A,D364A,F1049R,L2386F,E2393R,K84A,K240A,E360A,K363A,D364A,F1049R,L2386F,E2393R ;	ZN ZINC ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；pH 6.5；298 K；Sodium Cacodylate 100 mM pH 6.5, PEG 8000 5%, 2-methyl-2,4-pentanediol 40%	Resolution 2.03 Å R-free 0.242
6SLM Crystal structure of full-length HPV31 E6 oncoprotein in complex with LXXLL peptide of ubiquitin ligase E6AP Deposited 2019-08-20	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric	Chain A 403–417（15 aa）	Not recorded	ZN ZINC ION × 2 GOL GLYCEROL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；200mM tri-lithium citrate, 20% PEG 33350 protein concentration: 30mg/ml cryo condition: 35% glycerol	Resolution 2.80 Å R-free 0.268
6TGK Domain swapped E6AP C-lobe dimer Deposited 2019-11-16	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain C 765–869（105 aa）	Not recorded	ACT ACETATE ION × 4 CA CALCIUM ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.6；293 K；0.1 M CaCl 0.1 M Sodiumacetat 30% PEG400	Resolution 1.30 Å R-free 0.207
6U19 Solution Structure of the RAZUL domain from 26S proteasome subunit hRpn10/S5a complexed with the AZUL domain from E3 ligase E6AP/UBE3A Deposited 2019-08-15	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 24–87（64 aa） Fragment：UNP Residues 24-87	Not recorded	ZN ZINC ION × 1	SOLUTION NMR NMR measurement conditions pH 6.5；298 K；Ionic strength (raw mmCIF value) 50；Pressure 1 NMR sample composition 0.5 mM [U-100% 13C; U-100% 15N; U-35% 2H] 26S proteasome non-ATPase regulatory subunit 4 (305-377), 0.75 mM Ubiquitin-protein ligase E3A (24-87), 10 mM MOPS, 50 mM sodium chloride, 5 mM DTT, 10 uM zinc sulphate, 0.1 % sodium azide, 1 mM pefabloc, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 0.5 mM [U-100% 13C; U-100% 15N; U-35% 2H] 26S proteasome non-ATPase regulatory subunit 4 (305-377), 0.75 mM Ubiquitin-protein ligase E3A (24-87), 10 mM MOPS, 50 mM sodium chloride, 5 mM DTT, 10 uM zinc sulphate, 0.1 % sodium azide, 1 mM pefabloc, 100% D2O \| 100% D2O NMR sample composition 0.5 mM [U-100% 13C; U-100% 15N] Ubiquitin-protein ligase E3A (24-87), 0.75 mM 26S proteasome non-ATPase regulatory subunit 4 (305-377), 10 mM MOPS, 50 mM sodium chloride, 5 mM DTT, 10 uM zinc sulphate, 0.1 % sodium azide, 1 mM pefabloc, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 0.5 mM [U-100% 13C; U-100% 15N] Ubiquitin-protein ligase E3A (24-87), 0.75 mM 26S proteasome non-ATPase regulatory subunit 4 (305-377), 10 mM MOPS, 50 mM sodium chloride, 5 mM DTT, 10 uM zinc sulphate, 0.1 % sodium azide, 1 mM pefabloc, 100% D2O \| 100% D2O	Resolution not provided
7QPB Catalytic C-lobe of the HECT-type ubiquitin ligase E6AP in complex with a hybrid foldamer-peptide macrocycle Deposited 2022-01-03	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 741–852（112 aa） Chain C 741–852（112 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；277 K；12% PEG 8000, 0.1 M sodium cacodylate, 0.1 M calcium acetate pH 5.5	Resolution 2.34 Å R-free 0.263
7QPB Catalytic C-lobe of the HECT-type ubiquitin ligase E6AP in complex with a hybrid foldamer-peptide macrocycle Deposited 2022-01-03	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain A 741–852（112 aa） Chain C 741–852（112 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；277 K；12% PEG 8000, 0.1 M sodium cacodylate, 0.1 M calcium acetate pH 5.5	Resolution 2.34 Å R-free 0.263
7QPB Catalytic C-lobe of the HECT-type ubiquitin ligase E6AP in complex with a hybrid foldamer-peptide macrocycle Deposited 2022-01-03	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain B 741–852（112 aa） Chain D 741–852（112 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；277 K；12% PEG 8000, 0.1 M sodium cacodylate, 0.1 M calcium acetate pH 5.5	Resolution 2.34 Å R-free 0.263
7QPB Catalytic C-lobe of the HECT-type ubiquitin ligase E6AP in complex with a hybrid foldamer-peptide macrocycle Deposited 2022-01-03	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain B 741–852（112 aa） Chain D 741–852（112 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；277 K；12% PEG 8000, 0.1 M sodium cacodylate, 0.1 M calcium acetate pH 5.5	Resolution 2.34 Å R-free 0.263
8ENP UBE3A isoform 3 AZUL Deposited 2022-09-30	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–84（84 aa）	Not recorded	ZN ZINC ION × 1	SOLUTION NMR NMR measurement conditions pH 6；298 K；Ionic strength (raw mmCIF value) 450；Pressure 1 NMR sample composition 1.7 mM [U-99% 13C; U-99% 15N] UBE3A iso 3 AZUL, 10 mM MOPS, 450 mM sodium chloride, 10 mM beta-mercaptoethanol, 10 uM zinc sulfate, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
8EPT UBE3A isoform 2 AZUL domain Deposited 2022-10-06	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–87（87 aa）	Not recorded	ZN ZINC ION × 1	SOLUTION NMR NMR measurement conditions pH 6；298 K；Ionic strength (raw mmCIF value) 450；Pressure 1 NMR sample composition 1.8 mM [U-99% 13C; U-99% 15N] UBE3A iso2 AZUL, 10 mM MOPS, 450 mM sodium chloride, 10 mM beta-mercaptoethanol, 10 uM zinc sulfate, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
8GCR HPV16 E6-E6AP-p53 complex Deposited 2023-03-02	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 3 PDB declaration: trimeric	Chain R 1–875（875 aa）	Not recorded	ZN ZINC ION × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.38 Å
8JRN Structure of E6AP-E6 complex in Att1 state Deposited 2023-06-17	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 1–875（875 aa） Chain C 1–875（875 aa）	Mutation：C843A Mutation：C843A	ZN ZINC ION × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.60 Å
8JRO Structure of E6AP-E6 complex in Att2 state Deposited 2023-06-17	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 1–875（875 aa） Chain C 1–875（875 aa）	Mutation：C843A Mutation：C843A	ZN ZINC ION × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.01 Å
8JRP Structure of E6AP-E6 complex in Att3 state Deposited 2023-06-17	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 1–875（875 aa） Chain C 1–875（875 aa）	Mutation：C843A Mutation：C843A	ZN ZINC ION × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.58 Å
8JRQ Structure of E6AP-E6 complex in Det1 state Deposited 2023-06-17	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 1–875（875 aa） Chain C 1–875（875 aa）	Mutation：C843A Mutation：C843A	ZN ZINC ION × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.15 Å
8JRR Structure of E6AP-E6 complex in Det2 state Deposited 2023-06-17	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 1–875（875 aa） Chain C 1–875（875 aa）	Mutation：T798A/D799A/C843A Mutation：T798A/D799A/C843A	ZN ZINC ION × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.35 Å
8R1F Monomeric E6AP-E6-p53 ternary complex Deposited 2023-11-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 1–875（875 aa）	Not recorded	ZN ZINC ION × 3	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.67 Å
8R1G Dimeric ternary structure of E6AP-E6-p53 Deposited 2023-11-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 6 PDB declaration: hexameric	Chain A 1–875（875 aa） Chain D 1–875（875 aa）	Not recorded	ZN ZINC ION × 6	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.99 Å
9CHT Human E3 ligase E6AP in complex with HPV16-E6 and p53 Deposited 2024-07-02	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 1–875（875 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.54 Å
9L3L Crystal structure of the C lobe of E6AP in complex with K48-linked diUb Deposited 2024-12-18	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain A 765–872（108 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；291 K；0.2 M Sodium citrate tribasic dihydrate, 0.1 M TRIS hydrochloride pH 8.5, 30% v/v Polyethylene glycol 400	Resolution 2.59 Å R-free 0.269
9VG5 NMR Solution Structure of the Monomeric Catalytic C-terminal Lobe of the E6AP HECT E3 Ubiquitin Ligase Deposited 2025-06-12	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 762–875（114 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7.7；298 K；Ionic strength (raw mmCIF value) 100；Pressure AMBIENT NMR sample composition 20 mM NaPi, 100 mM NaCl, 0.15 mM DSS, 5 mM DTT, 95% H2O/5% D2O \| 95% H2O/5% D2O	Resolution not provided

21 other PDB entries and 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	UBE3A_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–358； UniProt 495–852 Author chain B； PDBConstruct 1–358； UniProt 495–852 Author chain C； PDBConstruct 1–358； UniProt 495–852

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	1d5f
Deposition date deposition_date	1999-10-07
Structure title title	STRUCTURE OF E6AP: INSIGHTS INTO UBIQUITINATION PATHWAY
Keywords keywords	BILOBAL STRUCTURE, ELONGATED SHAPE, E3 LIGASE, LIGASE; LIGASE
Experimental Method method	X-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier	32.97 Å
Radius of gyration Rg (electron density) rg_electron	31.71 Å
Forward intensity I(0) i0	219956000.00
Molecular weight molecular_weight	121760.0 kDa
Excluded volume excluded_volume	153660 Å³
Envelope volume envelope_volume	194070 Å³
Hydration-shell volume shell_volume	49604 Å³
Envelope diameter envelope_diameter	103.7 Å
Shell Rg shell_rg	39.80 Å
Envelope Rg envelope_rg	31.65 Å
Shape Rg shape_rg	31.69 Å
Total Rg total_rg	32.46 Å
Total atoms total_atoms	8583
Residues n_residues	1050
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	103.0 Å
Rg (real space) rg_real	32.76 Å
Rg uncertainty (real space) rg_real_error	0.67 Å
I(0) (real space) i0_real	2.2000e+08
I(0) uncertainty (real space) i0_real_error	3.1600e+06
Rg (reciprocal space) rg_reciprocal	32.85 Å
I(0) (reciprocal space) i0_reciprocal	220000000.0000
Solution quality estimate total_estimate	0.8971
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	42.9 Å
Skewness Skewness skewness	0.173
Kurtosis Kurtosis kurtosis	-0.449
Angular range angular_range	— – 0.2400 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	60450000.0000
Real-space data points n_real_points	49
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.906; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.987; Smooth: 0.953

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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7. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (3 domains)

Domain ID domain_id	d1d5fa_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.148 — Hect, E3 ligase catalytic domain
Superfamily Superfamily superfamily	d.148.1 — Hect, E3 ligase catalytic domain
Family Family family	d.148.1.1 — Hect, E3 ligase catalytic domain

Domain ID domain_id	d1d5fb_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.148 — Hect, E3 ligase catalytic domain
Superfamily Superfamily superfamily	d.148.1 — Hect, E3 ligase catalytic domain
Family Family family	d.148.1.1 — Hect, E3 ligase catalytic domain

Domain ID domain_id	d1d5fc_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.148 — Hect, E3 ligase catalytic domain
Superfamily Superfamily superfamily	d.148.1 — Hect, E3 ligase catalytic domain
Family Family family	d.148.1.1 — Hect, E3 ligase catalytic domain

CATH v4.4 (9 domains)

Domain ID domain_id	1d5fA01
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	1750 — Hect, E3 ligase catalytic domain fold
Homologous superfamily homologous superfamily	10 — Hect, E3 ligase catalytic domains

Domain ID domain_id	1d5fA02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	2160 — Hect, E3 ligase catalytic domain
Homologous superfamily homologous superfamily	10 — Hect, E3 ligase catalytic domain

Domain ID domain_id	1d5fA03
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	2410 — Hect, E3 ligase catalytic fold
Homologous superfamily homologous superfamily	10 — Hect, E3 ligase catalytic domain

Domain ID domain_id	1d5fB01
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	1750 — Hect, E3 ligase catalytic domain fold
Homologous superfamily homologous superfamily	10 — Hect, E3 ligase catalytic domains

Domain ID domain_id	1d5fB02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	2160 — Hect, E3 ligase catalytic domain
Homologous superfamily homologous superfamily	10 — Hect, E3 ligase catalytic domain

Domain ID domain_id	1d5fB03
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	2410 — Hect, E3 ligase catalytic fold
Homologous superfamily homologous superfamily	10 — Hect, E3 ligase catalytic domain

Domain ID domain_id	1d5fC01
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	1750 — Hect, E3 ligase catalytic domain fold
Homologous superfamily homologous superfamily	10 — Hect, E3 ligase catalytic domains

Domain ID domain_id	1d5fC02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	2160 — Hect, E3 ligase catalytic domain
Homologous superfamily homologous superfamily	10 — Hect, E3 ligase catalytic domain

Domain ID domain_id	1d5fC03
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	2410 — Hect, E3 ligase catalytic fold
Homologous superfamily homologous superfamily	10 — Hect, E3 ligase catalytic domain

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8. Citations (1)

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Unit-cell length a length_a	101.500 Å
Unit-cell length b length_b	113.700 Å
Unit-cell length c length_c	125.200 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	12

Space group space_group	P 21 21 21
Space-group number int_tables_number	19
Crystal system crystal_system	—

Resolution resolution	2.800 Å
Low-resolution limit resolution_low	15.000 Å
R factor r_factor	0.2280
R_work r_work	0.2300
R_free r_free	0.2830

Description description	E6AP HECT CATALYTIC DOMAIN, E3 LIGASE
Molecular weight formula_weight	41540.4 kDa
EC 编号 ec_number	6.3.2.-
Source method src_method	man
Copy count entity_count	3

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C
Atom count atom_count	8583

STRUCTURE OF E6AP: INSIGHTS INTO UBIQUITINATION PATHWAY

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

E6AP HECT CATALYTIC DOMAIN, E3 LIGASE

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

6. Entities and Polymers Entities & Polymers (1)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

7. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (3 domains)

CATH v4.4 (9 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

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	Escherichia coli

fit	/app/data/saxs_computation/d5/1d5f/1d5f.fit
pddf	/app/data/pr_computation/d5/1d5f/1d5f.pr.out
profile	/app/data/saxs_computation/d5/1d5f/1d5f.dat