SAXSdb — 6c95

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

N-alpha-acetyltransferase 15, NatA auxiliary subunit

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 × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain A； UniProt 1–866	Not recorded	N-alpha-acetyltransferase 10 × 1 （P41227） Huntingtin-interacting protein K × 1 （Q9NX55） IHP INOSITOL HEXAKISPHOSPHATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；19.5% PEG3350, 11% Tascimate, pH 6.5	Resolution 3.15 Å R-free 0.255

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 6C95	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
6C9M The Human NatA (Naa10/Naa15) amino-terminal acetyltransferase complex Deposited 2018-01-26	Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–866（866 aa）	Not recorded	IHP INOSITOL HEXAKISPHOSPHATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；16% PEG3350, 10% Tascimate, pH 7.5, 2% acetone	Resolution 2.80 Å R-free 0.242
6C9M The Human NatA (Naa10/Naa15) amino-terminal acetyltransferase complex Deposited 2018-01-26	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 1–866（866 aa）	Not recorded	IHP INOSITOL HEXAKISPHOSPHATE × 1 1PE PENTAETHYLENE GLYCOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；16% PEG3350, 10% Tascimate, pH 7.5, 2% acetone	Resolution 2.80 Å R-free 0.242
6PPL Cryo-EM structure of human NatE complex (NatA/Naa50) Deposited 2019-07-08	Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain B 1–866（866 aa）	Not recorded	ACO ACETYL COENZYME A × 2 IHP* INOSITOL HEXAKISPHOSPHATE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.02 Å
6PW9 Cryo-EM structure of human NatE/HYPK complex Deposited 2019-07-22	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 B 1–866（866 aa）	Not recorded	IHP INOSITOL HEXAKISPHOSPHATE × 1 ACO ACETYL COENZYME *A × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.03 Å
9F1B Mammalian ternary complex of a translating 80S ribosome, NAC and NatA/E Deposited 2024-04-18	Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 83 PDB declaration: 89-meric	Chain DB 1–866（866 aa）	Not recorded	MG MAGNESIUM ION × 420 ZN ZINC ION × 8 UNX UNKNOWN LIGAND × 306 IHP INOSITOL HEXAKISPHOSPHATE × 1 SPD SPERMIDINE × 30 SPM SPERMINE × 3 GTP GUANOSINE-5'-TRIPHOSPHATE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 3.01 Å
9F1C Mammalian quaternary complex of a translating 80S ribosome, NAC, MetAP1 and NatA/E Deposited 2024-04-18	Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 84 PDB declaration: 90-meric	Chain DB 1–866（866 aa）	Not recorded	UNX UNKNOWN LIGAND × 277 MG MAGNESIUM ION × 420 GTP GUANOSINE-5'-TRIPHOSPHATE × 1 SPD SPERMIDINE × 30 SPM SPERMINE × 3 ZN ZINC ION × 8 IHP INOSITOL HEXAKISPHOSPHATE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 3.78 Å
9F1D Mammalian quaternary complex of a translating 80S ribosome, NAC, MetAP1 and NatA/E-HYPK Deposited 2024-04-18	Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–RNA Heteromer；Protein × 85 PDB declaration: 91-meric	Chain DB 1–866（866 aa）	Not recorded	UNX UNKNOWN LIGAND × 295 SPD SPERMIDINE × 30 MG MAGNESIUM ION × 420 SPM SPERMINE × 3 GTP GUANOSINE-5'-TRIPHOSPHATE × 1 IHP INOSITOL HEXAKISPHOSPHATE × 1 ZN ZINC ION × 8	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 3.26 Å
9FPZ Human NatA-MAP2 80S ribosome complex Deposited 2024-06-14	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–RNA Heteromer；Protein × 11 PDB declaration: 13-meric	Chain B 1–841（841 aa）	Not recorded	CO COBALT (II) ION × 2 IHP INOSITOL HEXAKISPHOSPHATE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.69 Å
9FQ0 Human NatA-NAC-MAP1 80S ribosome complex Deposited 2024-06-14	Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–RNA Heteromer；Protein × 14 PDB declaration: hexadecameric	Chain B 1–841（841 aa）	Not recorded	IHP INOSITOL HEXAKISPHOSPHATE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.67 Å
9GJ5 Human 80S ribosome in complex with NatA in distal position and Ebp1 Deposited 2024-08-21	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–RNA Heteromer；Protein × 11 PDB declaration: 13-meric	Chain B 1–841（841 aa）	Not recorded	KGN D-chiro inositol hexakisphosphate × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.61 Å
9GJ6 Human 80S ribosome in complex with NatA in proximal and distal position Deposited 2024-08-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–RNA Heteromer；Protein × 15 PDB declaration: 17-meric	Chain B 1–841（841 aa） Chain D 1–841（841 aa）	Not recorded	IHP INOSITOL HEXAKISPHOSPHATE × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.91 Å
9QQB Quaternary complex of a translating ribosome, NAC, NMT1, and NatA Deposited 2025-03-31	Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–RNA Heteromer；Protein × 84 PDB declaration: 89-meric	Chain XA 1–866（866 aa）	Not recorded	SPD SPERMIDINE × 30 SPM SPERMINE × 3 MG MAGNESIUM ION × 412 UNX UNKNOWN LIGAND × 168 ZN ZINC ION × 8 IHP INOSITOL HEXAKISPHOSPHATE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.6 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 3.43 Å

11 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	NAA15_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–866； UniProt 1–866

N-alpha-acetyltransferase 10

Homo sapiens

UniProt P41227

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 × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain B； UniProt 1–235	Non-standard monomer：Yes (specific site not provided by mmCIF)	N-alpha-acetyltransferase 15, NatA auxiliary subunit × 1 （Q9BXJ9） Huntingtin-interacting protein K × 1 （Q9NX55） IHP INOSITOL HEXAKISPHOSPHATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；19.5% PEG3350, 11% Tascimate, pH 6.5	Resolution 3.15 Å R-free 0.255

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 6C95	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
6C9M The Human NatA (Naa10/Naa15) amino-terminal acetyltransferase complex Deposited 2018-01-26	Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1–235（235 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	IHP INOSITOL HEXAKISPHOSPHATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；16% PEG3350, 10% Tascimate, pH 7.5, 2% acetone	Resolution 2.80 Å R-free 0.242
6C9M The Human NatA (Naa10/Naa15) amino-terminal acetyltransferase complex Deposited 2018-01-26	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 1–235（235 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	IHP INOSITOL HEXAKISPHOSPHATE × 1 1PE PENTAETHYLENE GLYCOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；16% PEG3350, 10% Tascimate, pH 7.5, 2% acetone	Resolution 2.80 Å R-free 0.242
6PPL Cryo-EM structure of human NatE complex (NatA/Naa50) Deposited 2019-07-08	Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain C 1–235（235 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	ACO ACETYL COENZYME A × 2 IHP* INOSITOL HEXAKISPHOSPHATE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.02 Å
6PW9 Cryo-EM structure of human NatE/HYPK complex Deposited 2019-07-22	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 C 1–235（235 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	IHP INOSITOL HEXAKISPHOSPHATE × 1 ACO ACETYL COENZYME *A × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.03 Å
9F1B Mammalian ternary complex of a translating 80S ribosome, NAC and NatA/E Deposited 2024-04-18	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 × 83 PDB declaration: 89-meric	Chain DC 1–235（235 aa）	Mutation：E24Q, Y26F	MG MAGNESIUM ION × 420 ZN ZINC ION × 8 UNX UNKNOWN LIGAND × 306 IHP INOSITOL HEXAKISPHOSPHATE × 1 SPD SPERMIDINE × 30 SPM SPERMINE × 3 GTP GUANOSINE-5'-TRIPHOSPHATE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 3.01 Å
9F1C Mammalian quaternary complex of a translating 80S ribosome, NAC, MetAP1 and NatA/E Deposited 2024-04-18	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 × 84 PDB declaration: 90-meric	Chain DC 1–235（235 aa）	Mutation：E24Q, Y26F	UNX UNKNOWN LIGAND × 277 MG MAGNESIUM ION × 420 GTP GUANOSINE-5'-TRIPHOSPHATE × 1 SPD SPERMIDINE × 30 SPM SPERMINE × 3 ZN ZINC ION × 8 IHP INOSITOL HEXAKISPHOSPHATE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 3.78 Å
9F1D Mammalian quaternary complex of a translating 80S ribosome, NAC, MetAP1 and NatA/E-HYPK Deposited 2024-04-18	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–RNA Heteromer；Protein × 85 PDB declaration: 91-meric	Chain DC 1–235（235 aa）	Mutation：E24Q, Y26F	UNX UNKNOWN LIGAND × 295 SPD SPERMIDINE × 30 MG MAGNESIUM ION × 420 SPM SPERMINE × 3 GTP GUANOSINE-5'-TRIPHOSPHATE × 1 IHP INOSITOL HEXAKISPHOSPHATE × 1 ZN ZINC ION × 8	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 3.26 Å
9FPZ Human NatA-MAP2 80S ribosome complex Deposited 2024-06-14	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–RNA Heteromer；Protein × 11 PDB declaration: 13-meric	Chain 2 2–170（169 aa）	Not recorded	CO COBALT (II) ION × 2 IHP INOSITOL HEXAKISPHOSPHATE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.69 Å
9FQ0 Human NatA-NAC-MAP1 80S ribosome complex Deposited 2024-06-14	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–RNA Heteromer；Protein × 14 PDB declaration: hexadecameric	Chain 2 2–170（169 aa）	Not recorded	IHP INOSITOL HEXAKISPHOSPHATE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.67 Å
9GJ5 Human 80S ribosome in complex with NatA in distal position and Ebp1 Deposited 2024-08-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–RNA Heteromer；Protein × 11 PDB declaration: 13-meric	Chain 2 2–170（169 aa）	Not recorded	KGN D-chiro inositol hexakisphosphate × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.61 Å
9GJ6 Human 80S ribosome in complex with NatA in proximal and distal position Deposited 2024-08-21	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–RNA Heteromer；Protein × 15 PDB declaration: 17-meric	Chain A 1–235（235 aa） Chain C 1–235（235 aa）	Not recorded	IHP INOSITOL HEXAKISPHOSPHATE × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.91 Å
9QQB Quaternary complex of a translating ribosome, NAC, NMT1, and NatA Deposited 2025-03-31	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–RNA Heteromer；Protein × 84 PDB declaration: 89-meric	Chain XB 1–235（235 aa）	Not recorded	SPD SPERMIDINE × 30 SPM SPERMINE × 3 MG MAGNESIUM ION × 412 UNX UNKNOWN LIGAND × 168 ZN ZINC ION × 8 IHP INOSITOL HEXAKISPHOSPHATE × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7.6 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 3.43 Å

11 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	NAA10_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 2–236； UniProt 1–235

Huntingtin-interacting protein K

Homo sapiens

UniProt Q9NX55

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 × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain D； UniProt 1–129	Not recorded	N-alpha-acetyltransferase 15, NatA auxiliary subunit × 1 （Q9BXJ9） N-alpha-acetyltransferase 10 × 1 （P41227） IHP INOSITOL HEXAKISPHOSPHATE × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；19.5% PEG3350, 11% Tascimate, pH 6.5	Resolution 3.15 Å R-free 0.255

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 6C95	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
6PW9 Cryo-EM structure of human NatE/HYPK complex Deposited 2019-07-22	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 D 1–129（129 aa）	Not recorded	IHP INOSITOL HEXAKISPHOSPHATE × 1 ACO ACETYL COENZYME *A × 1	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.03 Å
9F1D Mammalian quaternary complex of a translating 80S ribosome, NAC, MetAP1 and NatA/E-HYPK Deposited 2024-04-18	Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–RNA Heteromer；Protein × 85 PDB declaration: 91-meric	Chain DD 1–121（121 aa）	Not recorded	UNX UNKNOWN LIGAND × 295 SPD SPERMIDINE × 30 MG MAGNESIUM ION × 420 SPM SPERMINE × 3 GTP GUANOSINE-5'-TRIPHOSPHATE × 1 IHP INOSITOL HEXAKISPHOSPHATE × 1 ZN ZINC ION × 8	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE-PROPANE	Resolution 3.26 Å

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

View Construct and Data Evidence

UniProt name	HYPK_HUMAN
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain D； PDBConstruct 1–129； UniProt 1–129

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	6c95
Deposition date deposition_date	2018-01-25
Structure title title	The Human NatA (Naa10/Naa15) amino-terminal acetyltransferase complex bound to HYPK
Keywords keywords	NatA, HYPK, N-terminal acetylation, Huntingtin interacting protein, protein complex, TRANSFERASE; TRANSFERASE
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	33.25 Å
Radius of gyration Rg (electron density) rg_electron	32.37 Å
Forward intensity I(0) i0	226347000.00
Molecular weight molecular_weight	120010.0 kDa
Excluded volume excluded_volume	150240 Å³
Envelope volume envelope_volume	198320 Å³
Hydration-shell volume shell_volume	49379 Å³
Envelope diameter envelope_diameter	111.8 Å
Shell Rg shell_rg	40.59 Å
Envelope Rg envelope_rg	32.05 Å
Shape Rg shape_rg	32.36 Å
Total Rg total_rg	33.06 Å
Total atoms total_atoms	8420
Residues n_residues	1028
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	102.9 Å
Rg (real space) rg_real	33.02 Å
Rg uncertainty (real space) rg_real_error	0.59 Å
I(0) (real space) i0_real	2.2630e+08
I(0) uncertainty (real space) i0_real_error	3.1640e+06
Rg (reciprocal space) rg_reciprocal	33.12 Å
I(0) (reciprocal space) i0_reciprocal	226400000.0000
Solution quality estimate total_estimate	0.9028
Solution quality rating solution_quality	EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	42.9 Å
Skewness Skewness skewness	0.128
Kurtosis Kurtosis kurtosis	-0.482
Angular range angular_range	— – 0.2400 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	42160000.0000
Real-space data points n_real_points	49
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.930; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.989; Smooth: 0.952

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Description description	N-alpha-acetyltransferase 15, NatA auxiliary subunit
Molecular weight formula_weight	101427.6 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	8454

MPAVSLPPKENALFKRILRCYEHKQYRNGLKFCKQILSNPKFAEHGETLAMKGLTLNCLGKKEEAYELVRRGLRNDLKSHVCWHVYGLLQRSDKKYDEAIKCYRNALKWDKDNLQILRDLSLLQIQMRDLEGYRETRYQLLQLRPAQRASWIGYAIAYHLLEDYEMAAKILEEFRKTQQTSPDKVDYEYSELLLYQNQVLREAGLYREALEHLCTYEKQICDKLAVEETKGELLLQLCRLEDAADVYRGLQERNPENWAYYKGLEKALKPANMLERLKIYEEAWTKYPRGLVPRRLPLNFLSGEKFKECLDKFLRMNFSKGCPPVFNTLRSLYKDKEKVAIIEELVVGYETSLKSCRLFNPNDDGKEEPPTTLLWVQYYLAQHYDKIGQPSIALEYINTAIESTPTLIELFLVKAKIYKHAGNIKEAARWMDEAQALDTADRFINSKCAKYMLKANLIKEAEEMCSKFTREGTSAVENLNEMQCMWFQTECAQAYKAMNKFGEALKKCHEIERHFIEITDDQFDFHTYCMRKITLRSYVDLLKLEDVLRQHPFYFKAARIAIEIYLKLHDNPLTDENKEHEADTANMSDKELKKLRNKQRRAQKKAQIEEEKKNAEKEKQQRNQKKKKDDDDEEIGGPKEELIPEKLAKVETPLEEAIKFLTPLKNLVKNKIETHLFAFEIYFRKEKFLLMLQSVKRAFAIDSSHPWLHECMIRLFNTAVCESKDLSDTVRTVLKQEMNRLFGATNPKNFNETFLKRNSDSLPHRLSAAKMVYYLDPSSQKRAIELATTLDESLTNRNLQTCMEVLEALYDGSLGDCKEAAEIYRANCHKLFPYALAFMPPGYEEDMKITVNGDSSAEAEELANEI

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

Entity 2 Entity 2 polymer

Description description	N-alpha-acetyltransferase 10
Molecular weight formula_weight	26522.6 kDa
EC 编号 ec_number	2.3.1.255
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B

XMNIRNARPEDLMNMQHCNLLCLPENYQMKYYFYHGLSWPQLSYIAEDENGKIVGYVLAKMEEDPDDVPHGHITSLAVKRSHRRLGLAQKLMDQASRAMIENFNAKYVSLHVRKSNRAALHLYSNTLNFQISEVEPKYYADGEDAYAMKRDLTQMADELRRHLELKEKGRHVVLGAIENKVESKGNSPPSSGEACREEKGLAAEDSGGDSKDLSEVSETTESTDVKDSSEASDSAS

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

Entity 3 Entity 3 polymer

Description description	Huntingtin-interacting protein K
Molecular weight formula_weight	14689.5 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	D

MRRRGEIDMATEGDVELELETETSGPERPPEKPRKHDSGAADLERVTDYAEEKEIQSSNLETAMSVIGDRRSREQKAKQEREKELAKVTIKKEDLELIMTEMEISRAAAERSLREHMGNVVEALIALTN

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

Entity 4 Entity 4 non-polymer

Description description	INOSITOL HEXAKISPHOSPHATE
Molecular weight formula_weight	660.0 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 5 Entity 5 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	34

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d6c95b_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.108 — Acyl-CoA N-acyltransferases (Nat)
Superfamily Superfamily superfamily	d.108.1 — Acyl-CoA N-acyltransferases (Nat)
Family Family family	d.108.1.0 — automated matches

CATH v4.4 (1 domains)

Domain ID domain_id	6c95B00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	630 — Aminopeptidase
Homologous superfamily homologous superfamily	30 — Gcn5-related N-acetyltransferase (GNAT)

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8. Citations (1)

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Unit-cell length a length_a	182.320 Å
Unit-cell length b length_b	182.320 Å
Unit-cell length c length_c	86.070 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	120.00 °
Molecules per unit cell Z z_pdb	6

Space group space_group	P 63
Space-group number int_tables_number	173
Crystal system crystal_system	—

Resolution resolution	3.150 Å
Low-resolution limit resolution_low	49.040 Å
R factor r_factor	0.2230
R_work r_work	0.2210
R_free r_free	0.2550

fit	/app/data/saxs_computation/c9/6c95/6c95.fit
pddf	/app/data/pr_computation/c9/6c95/6c95.pr.out
profile	/app/data/saxs_computation/c9/6c95/6c95.dat

The Human NatA (Naa10/Naa15) amino-terminal acetyltransferase complex bound to HYPK

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

N-alpha-acetyltransferase 15, NatA auxiliary subunit

State in the Current Structure

Other States of the Same Protein in the Database

N-alpha-acetyltransferase 10

State in the Current Structure

Other States of the Same Protein in the Database

Huntingtin-interacting protein K

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

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (5)

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 non-polymer

Entity 5 Entity 5 water

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

CATH v4.4 (1 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)