SAXSdb — 9bax

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

Protein EFR3 homolog A

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 × 8 PDB declaration: octameric（8） Consistent with protein copy count	Chain C； UniProt 721–791 Chain H； UniProt 721–791	Not recorded	Phosphatidylinositol 4-kinase alpha × 2 （P42356） Tetratricopeptide repeat protein 7B × 2 （Q86TV6） Hyccin × 2 （Q9BYI3）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7；Freshly prepared gel filtration buffer, filtered through 0.22um filter and degassed cryo-EM vitrification conditions：Cryogen ETHANE；Blot force -5, blot time 1.5 s	Resolution 3.65 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence

UniProt name	EFR3A_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain C； PDBConstruct 60–130； UniProt 721–791 Author chain H； PDBConstruct 60–130； UniProt 721–791

Phosphatidylinositol 4-kinase alpha

Homo sapiens

UniProt P42356

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 × 8 PDB declaration: octameric（8） Consistent with protein copy count	Chain A； UniProt 1–2102 Chain B； UniProt 1–2102	Not recorded	Protein EFR3 homolog A × 2 （Q14156） Tetratricopeptide repeat protein 7B × 2 （Q86TV6） Hyccin × 2 （Q9BYI3）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7；Freshly prepared gel filtration buffer, filtered through 0.22um filter and degassed cryo-EM vitrification conditions：Cryogen ETHANE；Blot force -5, blot time 1.5 s	Resolution 3.65 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 9BAX	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
6BQ1 Human PI4KIIIa lipid kinase complex Deposited 2017-11-27	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain A 932–2102（1171 aa） Chain E 932–2102（1171 aa）	Not recorded	E4S 5-{2-amino-1-[4-(morpholin-4-yl)phenyl]-1H-benzimidazol-6-yl}-N-(2-fluorophenyl)-2-methoxypyridine-3-sulfonamide × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.60 Å
9B9G Structure of the PI4KA complex bound to Calcineurin Deposited 2024-04-02	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 10 PDB declaration: decameric	Chain A 1–2102（2102 aa） Chain B 1–2102（2102 aa）	Not recorded	CA CALCIUM ION × 8	ELECTRON MICROSCOPY cryo-EM buffer pH 7；Freshly prepared gel filtration buffer, filtered through 0.22um filter and degassed cryo-EM vitrification conditions Cryogen ETHANE；Blot force -5, blot time 1 s	Resolution 3.50 Å
9OT6 Cryo-EM structure of the PI4KA complex bound to an EFR3 interfering nanobody (F3IN) Deposited 2025-05-26	Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain A 1–2102（2102 aa） Chain B 1–2102（2102 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE；Blot force -5, blot time 1.5 s.	Resolution 3.54 Å

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

View Construct and Data Evidence

UniProt name	PI4KA_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain A； PDBConstruct 1–2102； UniProt 1–2102 Author chain B； PDBConstruct 1–2102； UniProt 1–2102

Tetratricopeptide repeat protein 7B

Homo sapiens

UniProt Q86TV6

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 × 8 PDB declaration: octameric（8） Consistent with protein copy count	Chain D； UniProt 1–843 Chain F； UniProt 1–843	Not recorded	Protein EFR3 homolog A × 2 （Q14156） Phosphatidylinositol 4-kinase alpha × 2 （P42356） Hyccin × 2 （Q9BYI3）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7；Freshly prepared gel filtration buffer, filtered through 0.22um filter and degassed cryo-EM vitrification conditions：Cryogen ETHANE；Blot force -5, blot time 1.5 s	Resolution 3.65 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 9BAX	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
5DSE Crystal Structure of the TTC7B/Hyccin Complex Deposited 2015-09-17	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 7–843（837 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；1.35 ul protein + 1.35 ul mother liquor (0.1 M HEPES [pH 7.0-7.4], 4-5% polyethylene glycol [PEG] 8,000) + 0.3 ul 0.2 M 3-(1-Pyridino)-1-propane sulfonate (NDSB-201)	Resolution 2.90 Å R-free 0.242
5DSE Crystal Structure of the TTC7B/Hyccin Complex Deposited 2015-09-17	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 7–843（837 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；1.35 ul protein + 1.35 ul mother liquor (0.1 M HEPES [pH 7.0-7.4], 4-5% polyethylene glycol [PEG] 8,000) + 0.3 ul 0.2 M 3-(1-Pyridino)-1-propane sulfonate (NDSB-201)	Resolution 2.90 Å R-free 0.242
6BQ1 Human PI4KIIIa lipid kinase complex Deposited 2017-11-27	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain B 1–843（843 aa） Chain F 1–843（843 aa）	Not recorded	E4S 5-{2-amino-1-[4-(morpholin-4-yl)phenyl]-1H-benzimidazol-6-yl}-N-(2-fluorophenyl)-2-methoxypyridine-3-sulfonamide × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.60 Å
9B9G Structure of the PI4KA complex bound to Calcineurin Deposited 2024-04-02	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 10 PDB declaration: decameric	Chain D 1–843（843 aa） Chain F 1–843（843 aa）	Not recorded	CA CALCIUM ION × 8	ELECTRON MICROSCOPY cryo-EM buffer pH 7；Freshly prepared gel filtration buffer, filtered through 0.22um filter and degassed cryo-EM vitrification conditions Cryogen ETHANE；Blot force -5, blot time 1 s	Resolution 3.50 Å
9OT6 Cryo-EM structure of the PI4KA complex bound to an EFR3 interfering nanobody (F3IN) Deposited 2025-05-26	Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain D 1–843（843 aa） Chain F 1–843（843 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE；Blot force -5, blot time 1.5 s.	Resolution 3.54 Å

4 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	TTC7B_HUMAN
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain D； PDBConstruct 1–843； UniProt 1–843 Author chain F； PDBConstruct 1–843； UniProt 1–843

Hyccin

Homo sapiens

UniProt Q9BYI3

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 × 8 PDB declaration: octameric（8） Consistent with protein copy count	Chain E； UniProt 1–308 Chain G； UniProt 1–308	Not recorded	Protein EFR3 homolog A × 2 （Q14156） Phosphatidylinositol 4-kinase alpha × 2 （P42356） Tetratricopeptide repeat protein 7B × 2 （Q86TV6）	ELECTRON MICROSCOPY cryo-EM buffer：pH 7；Freshly prepared gel filtration buffer, filtered through 0.22um filter and degassed cryo-EM vitrification conditions：Cryogen ETHANE；Blot force -5, blot time 1.5 s	Resolution 3.65 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 9BAX	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
5DSE Crystal Structure of the TTC7B/Hyccin Complex Deposited 2015-09-17	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 2–308（307 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；1.35 ul protein + 1.35 ul mother liquor (0.1 M HEPES [pH 7.0-7.4], 4-5% polyethylene glycol [PEG] 8,000) + 0.3 ul 0.2 M 3-(1-Pyridino)-1-propane sulfonate (NDSB-201)	Resolution 2.90 Å R-free 0.242
5DSE Crystal Structure of the TTC7B/Hyccin Complex Deposited 2015-09-17	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 2–308（307 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；1.35 ul protein + 1.35 ul mother liquor (0.1 M HEPES [pH 7.0-7.4], 4-5% polyethylene glycol [PEG] 8,000) + 0.3 ul 0.2 M 3-(1-Pyridino)-1-propane sulfonate (NDSB-201)	Resolution 2.90 Å R-free 0.242
6BQ1 Human PI4KIIIa lipid kinase complex Deposited 2017-11-27	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain C 2–289（288 aa） Chain G 2–289（288 aa）	Not recorded	E4S 5-{2-amino-1-[4-(morpholin-4-yl)phenyl]-1H-benzimidazol-6-yl}-N-(2-fluorophenyl)-2-methoxypyridine-3-sulfonamide × 2	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.60 Å
9B9G Structure of the PI4KA complex bound to Calcineurin Deposited 2024-04-02	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 10 PDB declaration: decameric	Chain E 1–308（308 aa） Chain G 1–308（308 aa）	Not recorded	CA CALCIUM ION × 8	ELECTRON MICROSCOPY cryo-EM buffer pH 7；Freshly prepared gel filtration buffer, filtered through 0.22um filter and degassed cryo-EM vitrification conditions Cryogen ETHANE；Blot force -5, blot time 1 s	Resolution 3.50 Å
9OT6 Cryo-EM structure of the PI4KA complex bound to an EFR3 interfering nanobody (F3IN) Deposited 2025-05-26	Different construct Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain E 1–308（308 aa） Fragment：residues 1-308 Chain G 1–308（308 aa） Fragment：residues 1-308	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7 cryo-EM vitrification conditions Cryogen ETHANE；Blot force -5, blot time 1.5 s.	Resolution 3.54 Å

4 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	HYCCI_HUMAN
Isoform	—
PDB entities	4
Chains and sequence ranges	Author chain E； PDBConstruct 1–308； UniProt 1–308 Author chain G； PDBConstruct 1–308； UniProt 1–308

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	9bax
Deposition date deposition_date	2024-04-04
Structure title title	PI4KA complex bound to C-terminus of EFR3A
Keywords keywords	PI4KA, TTC7B, FAM126A, EFR3A, EFR3, Lipid Signaling, PI4KIIIa, Phosphoinositide Kinase, SIGNALING PROTEIN; SIGNALING 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	76.57 Å
Radius of gyration Rg (electron density) rg_electron	76.88 Å
Forward intensity I(0) i0	4604430000.00
Molecular weight molecular_weight	598630.0 kDa
Excluded volume excluded_volume	758880 Å³
Envelope volume envelope_volume	1343500 Å³
Hydration-shell volume shell_volume	148190 Å³
Envelope diameter envelope_diameter	280.0 Å
Shell Rg shell_rg	71.87 Å
Envelope Rg envelope_rg	74.53 Å
Shape Rg shape_rg	76.87 Å
Total Rg total_rg	76.82 Å
Total atoms total_atoms	42100
Residues n_residues	5264
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	262.5 Å
Rg (real space) rg_real	79.99 Å
Rg uncertainty (real space) rg_real_error	1.59 Å
I(0) (real space) i0_real	4.6120e+09
I(0) uncertainty (real space) i0_real_error	9.9020e+07
Rg (reciprocal space) rg_reciprocal	76.13 Å
I(0) (reciprocal space) i0_reciprocal	4599000000.0000
Solution quality estimate total_estimate	0.8975
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	78.8 Å
Skewness Skewness skewness	0.448
Kurtosis Kurtosis kurtosis	-0.193
Angular range angular_range	— – 0.1000 Å⁻¹
Current regularization parameter α current_alpha	1.2480
Highest regularization parameter α highest_alpha	263000000.0000
Real-space data points n_real_points	21
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.929; Stabil: 0.867; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.312

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Description description	Protein EFR3 homolog A
Molecular weight formula_weight	14366.9 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C,H
Atom count atom_count	42100

MASAWSHPQFEKGGGSGGGSGGSAWSHPQFEKSGMHHHHHHHHHHGSGGSENLYFQGAGSNTEEITFEALKKAIDTSGMEEQEKEKRRLVIEKFQKAPFEEIAAQCESKANLLHDRLAQILELTIRPPPS

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	Escherichia coli BL21(DE3)

Entity 2 Entity 2 polymer

Description description	Phosphatidylinositol 4-kinase alpha
Molecular weight formula_weight	237102.3 kDa
EC 编号 ec_number	2.7.1.67
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B,A

MAAAPARGGGGGGGGGGGCSGSGSSASRGFYFNTVLSLARSLAVQRPASLEKVQKLLCMCPVDFHGIFQLDERRRDAVIALGIFLIESDLQHKDCVVPYLLRLLKGLPKVYWVEESTARKGRGALPVAESFSFCLVTLLSDVAYRDPSLRDEILEVLLQVLHVLLGMCQALEIQDKEYLCKYAIPCLIGISRAFGRYSNMEESLLSKLFPKIPPHSLRVLEELEGVRRRSFNDFRSILPSNLLTVCQEGTLKRKTSSVSSISQVSPERGMPPPSSPGGSAFHYFEASCLPDGTALEPEYYFSTISSSFSVSPLFNGVTYKEFNIPLEMLRELLNLVKKIVEEAVLKSLDAIVASVMEANPSADLYYTSFSDPLYLTMFKMLRDTLYYMKDLPTSFVKEIHDFVLEQFNTSQGELQKILHDADRIHNELSPLKLRCQANAACVDLMVWAVKDEQGAENLCIKLSEKLQSKTSSKVIIAHLPLLICCLQGLGRLCERFPVVVHSVTPSLRDFLVIPSPVLVKLYKYHSQYHTVAGNDIKISVTNEHSESTLNVMSGKKSQPSMYEQLRDIAIDNICRCLKAGLTVDPVIVEAFLASLSNRLYISQESDKDAHLIPDHTIRALGHIAVALRDTPKVMEPILQILQQKFCQPPSPLDVLIIDQLGCLVITGNQYIYQEVWNLFQQISVKASSVVYSATKDYKDHGYRHCSLAVINALANIAANIQDEHLVDELLMNLLELFVQLGLEGKRASERASEKGPALKASSSAGNLGVLIPVIAVLTRRLPPIKEAKPRLQKLFRDFWLYSVLMGFAVEGSGLWPEEWYEGVCEIATKSPLLTFPSKEPLRSVLQYNSAMKNDTVTPAELSELRSTIINLLDPPPEVSALINKLDFAMSTYLLSVYRLEYMRVLRSTDPDRFQVMFCYFEDKAIQKDKSGMMQCVIAVADKVFDAFLNMMADKAKTKENEEELERHAQFLLVNFNHIHKRIRRVADKYLSGLVDKFPHLLWSGTVLKTMLDILQTLSLSLSADIHKDQPYYDIPDAPYRITVPDTYEARESIVKDFAARCGMILQEAMKWAPTVTKSHLQEYLNKHQNWVSGLSQHTGLAMATESILHFAGYNKQNTTLGATQLSERPACVKKDYSNFMASLNLRNRYAGEVYGMIRFSGTTGQMSDLNKMMVQDLHSALDRSHPQHYTQAMFKLTAMLISSKDCDPQLLHHLCWGPLRMFNEHGMETALACWEWLLAGKDGVEVPFMREMAGAWHMTVEQKFGLFSAEIKEADPLAASEASQPKPCPPEVTPHYIWIDFLVQRFEIAKYCSSDQVEIFSSLLQRSMSLNIGGAKGSMNRHVAAIGPRFKLLTLGLSLLHADVVPNATIRNVLREKIYSTAFDYFSCPPKFPTQGEKRLREDISIMIKFWTAMFSDKKYLTASQLVPPDNQDTRSNLDITVGSRQQATQGWINTYPLSSGMSTISKKSGMSKKTNRGSQLHKYYMKRRTLLLSLLATEIERLITWYNPLSAPELELDQAGENSVANWRSKYISLSEKQWKDNVNLAWSISPYLAVQLPARFKNTEAIGNEVTRLVRLDPGAVSDVPEAIKFLVTWHTIDADAPELSHVLCWAPTDPPTGLSYFSSMYPPHPLTAQYGVKVLRSFPPDAILFYIPQIVQALRYDKMGYVREYILWAASKSQLLAHQFIWNMKTNIYLDEEGHQKDPDIGDLLDQLVEEITGSLSGPAKDFYQREFDFFNKITNVSAIIKPYPKGDERKKACLSALSEVKVQPGCYLPSNPEAIVLDIDYKSGTPMQSAAKAPYLAKFKVKRCGVSELEKEGLRCRSDSEDECSTQEADGQKISWQAAIFKVGDDCRQDMLALQIIDLFKNIFQLVGLDLFVFPYRVVATAPGCGVIECIPDCTSRDQLGRQTDFGMYDYFTRQYGDESTLAFQQARYNFIRSMAAYSLLLFLLQIKDRHNGNIMLDKKGHIIHIDFGFMFESSPGGNLGWEPDIKLTDEMVMIMGGKMEATPFKWFMEMCVRGYLAVRPYMDAVVSLVTLMLDTGLPCFRGQTIKLLKHRFSPNMTEREAANFIMKVIQSCFLSNRSRTYDMIQYYQNDIPY

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	Tetratricopeptide repeat protein 7B
Molecular weight formula_weight	94294.1 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	F,D

MATKKAGSRLETEIERCRSECQWERIPELVKQLSAKLIANDDMAELLLGESKLEQYLKEHPLRQGASPRGPKPQLTEVRKHLTAALDRGNLKSEFLQESNLIMAKLNYVEGDYKEALNIYARVGLDDLPLTAVPPYRLRVIAEAYATKGLCLEKLPISSSTSNLHVDREQDVITCYEKAGDIALLYLQEIERVILSNIQNRSPKPGPAPHDQELGFFLETGLQRAHVLYFKNGNLTRGVGRFRELLRAVETRTTQNLRMTIARQLAEILLRGMCEQSYWNPLEDPPCQSPLDDPLRKGANTKTYTLTRRARVYSGENIFCPQENTEEALLLLLISESMANRDAVLSRIPEHKSDRLISLQSASVVYDLLTIALGRRGQYEMLSECLERAMKFAFEEFHLWYQFALSLMAAGKSARAVKVLKECIRLKPDDATIPLLAAKLCMGSLHWLEEAEKFAKTVVDVGEKTSEFKAKGYLALGLTYSLQATDASLRGMQEVLQRKALLAFQRAHSLSPTDHQAAFYLALQLAISRQIPEALGYVRQALQLQGDDANSLHLLALLLSAQKHYHDALNIIDMALSEYPENFILLFSKVKLQSLCRGPDEALLTCKHMLQIWKSCYNLTNPSDSGRGSSLLDRTIADRRQLNTITLPDFSDPETGSVHATSVAASRVEQALSEVASSLQSSAPKQGPLHPWMTLAQIWLHAAEVYIGIGKPAEATACTQEAANLFPMSHNVLYMRGQIAELRGSMDEARRWYEEALAISPTHVKSMQRLALILHQLGRYSLAEKILRDAVQVNSTAHEVWNGLGEVLQAQGNDAAATECFLTALELEASSPAVPFTIIPRVL

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 polymer

Description description	Hyccin
Molecular weight formula_weight	34638.9 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	G,E

MFTSEKGVVEEWLSEFKTLPETSLPNYATNLKDKSSLVSSLYKVIQEPQSELLEPVCHQLFEFYRSGEEQLLQFTLQFLPELIWCYLAVSASRNVHSSGCIEALLLGVYNLEIVDKQGHTKVLSFTIPSLSKPSVYHEPSSIGSMALTESALSQHGLSKVVYSGPHPQREMLTAQNRFEVLTFLLLCYNAALTYMPSVSLQSLCQICSRICVCGYPRQHVRKYKGISSRIPVSSGFMVQMLTGIYFAFYNGEWDLAQKALDDIIYRAQLELYPEPLLVANAIKASLPHGPMKSNKEGTRCIQVEITPT

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	3.65 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	135126

fit	/app/data/saxs_computation/ba/9bax/9bax.fit
pddf	/app/data/pr_computation/ba/9bax/9bax.pr.out
profile	/app/data/saxs_computation/ba/9bax/9bax.dat

PI4KA complex bound to C-terminus of EFR3A

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

Protein EFR3 homolog A

State in the Current Structure

Other States of the Same Protein in the Database

Phosphatidylinositol 4-kinase alpha

State in the Current Structure

Other States of the Same Protein in the Database

Tetratricopeptide repeat protein 7B

State in the Current Structure

Other States of the Same Protein in the Database

Hyccin

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 (4)

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

8. Citations (1)

9. Files and Curves (10)

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