6i7s

Microsomal triglyceride transfer protein

Method: X-RAY DIFFRACTION D_max: 215.9 Å Quality: GOOD

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

Protein disulfide-isomerase

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 × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 18–508	Not recorded	Microsomal triglyceride transfer protein large subunit × 1 （P55157） CA CALCIUM ION × 1 EDO 1,2-ETHANEDIOL × 11 PGE TRIETHYLENE GLYCOL × 1 SO4 SULFATE ION × 7 PEG DI(HYDROXYETHYL)ETHER × 2 PE5 3,6,9,12,15,18,21,24-OCTAOXAHEXACOSAN-1-OL × 1 TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 7.5；277 K；0.1 M Tris pH 8.25, 0.2 M Li2SO4, 32% v/v PEG 400, 2% Polypropylene glycol P425	Resolution 2.50 Å R-free 0.257
2	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain B； UniProt 18–508	Not recorded	Microsomal triglyceride transfer protein large subunit × 1 （P55157） CA CALCIUM ION × 1 EDO 1,2-ETHANEDIOL × 8 PGE TRIETHYLENE GLYCOL × 5 SO4 SULFATE ION × 4 PEG DI(HYDROXYETHYL)ETHER × 7 PE5 3,6,9,12,15,18,21,24-OCTAOXAHEXACOSAN-1-OL × 1 PE4 2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 7.5；277 K；0.1 M Tris pH 8.25, 0.2 M Li2SO4, 32% v/v PEG 400, 2% Polypropylene glycol P425	Resolution 2.50 Å R-free 0.257

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 6I7S	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1BJX HUMAN PROTEIN DISULFIDE ISOMERASE, NMR, 24 STRUCTURES Deposited 1998-06-29	Different construct 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 136–245（110 aa） Fragment：B DOMAIN	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.5；300 K	Resolution not provided
1MEK HUMAN PROTEIN DISULFIDE ISOMERASE, NMR, 40 STRUCTURES Deposited 1996-04-16	Different construct 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 18–137（120 aa） Fragment：PROLYL 4-HYDROXYLASE BETA SUBUNIT	Not recorded	No recorded non-water small molecule	SOLUTION NMR mmCIF provides none of the parsed conditions	Resolution not provided
1X5C The solution structure of the second thioredoxin-like domain of human Protein disulfide-isomerase Deposited 2005-05-15	Different construct 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 368–475（108 aa） Fragment：Thioredoxin like domain	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7；296 K；Ionic strength (raw mmCIF value) 120mM；Pressure ambient NMR sample composition 1.2mM thioredoxin like domain U-15N,13C; 20mM d-Tris HCl; 100mM NaCl; 1mM d-DTT; 0.02% NaN3; 10% D2O \| 90% H2O/10% D2O	Resolution not provided
2BJX PROTEIN DISULFIDE ISOMERASE Deposited 1999-01-30	Different construct 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 136–245（110 aa） Fragment：B DOMAIN	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.5；300 K；Pressure 1	Resolution not provided
2K18 Solution structure of bb' domains of human protein disulfide isomerase Deposited 2008-02-22	Different construct 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 135–357（223 aa） Fragment：residues 135-357	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7；303 K；Ionic strength (raw mmCIF value) 0.1；Pressure 1 NMR sample composition 2 mM [U-99% 13C; U-99% 15N] hPDI-bb, 25 mM sodium phosphate, 70 mM sodium chloride, 0.5 mM EDTA, 5 mM DTT, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 2 mM hPDI-bb, 25 mM sodium phosphate, 70 mM sodium chloride, 0.5 mM EDTA, 5 mM DTT, 100% D2O \| 100% D2O NMR sample composition 0.5 mM [U-99% 15N] hPDI-bb, 25 mM sodium phosphate, 70 mM sodium chloride, 0.5 mM EDTA, 5 mM DTT, 12 mg/mL Pf1 phages, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
3BJ5 Alternative conformations of the x region of human protein disulphide-isomerase modulate exposure of the substrate binding b' domain Deposited 2007-12-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 230–368（139 aa） Fragment：;b'x domain, UNPR residues 230-368 ;	Mutation：I272A	SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；295.15 K；2.95M Ammonium sulfate, 0.2M NaCl, 0.1M Tris-HCl pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 295.15K	Resolution 2.20 Å R-free 0.255
3UEM Crystal structure of human PDI bb'a' domains Deposited 2011-10-30	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 137–479（343 aa） Fragment：;bb'a' domains ;	Not recorded	D1D (4S,5S)-1,2-DITHIANE-4,5-DIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；289 K；25%(w/v) PEG3350, 0.1M Tris-HCl, 0.2M ammonium acetate, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 289K	Resolution 2.29 Å R-free 0.280
4EKZ Crystal structure of reduced hPDI (abb'xa') Deposited 2012-04-10	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 18–479（462 aa） Fragment：reduced full-length hPDI, UNP residues 18-479	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；pH 9.8；294 K；25% PEG 3350, 0.1M Bis-Tris, 0.2M ammonium acetate, pH 9.8, EVAPORATION, temperature 294K	Resolution 2.51 Å R-free 0.250
4EL1 Crystal structure of oxidized hPDI (abb'xa') Deposited 2012-04-10	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 18–479（462 aa） Fragment：oxidized full-length hPDI, UNP residues 18-479	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；pH 9.8；294 K；25% PEG 3350, 0.1M Bis-Tris, 0.2M ammonium acetate, pH 9.8, EVAPORATION, temperature 294K	Resolution 2.88 Å R-free 0.281
4EL1 Crystal structure of oxidized hPDI (abb'xa') Deposited 2012-04-10	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 18–479（462 aa） Fragment：oxidized full-length hPDI, UNP residues 18-479	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions EVAPORATION；pH 9.8；294 K；25% PEG 3350, 0.1M Bis-Tris, 0.2M ammonium acetate, pH 9.8, EVAPORATION, temperature 294K	Resolution 2.88 Å R-free 0.281
4JU5 Crystal structure of the dimeric form of the bb' domains of human protein disulfide isomerase Deposited 2013-03-24	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 A 135–367（233 aa） Fragment：;bb' domain ; Chain B 135–367（233 aa） Fragment：;bb' domain ;	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4；295 K；25% (w/v) polyethylene glycol 1500, 25 mM sodium malonate, 37.5 mM imidazole, 37.5 mM boric acid, pH 4.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K	Resolution 2.28 Å R-free 0.290
7ZSC Crystal structure of the heterodimeric human C-P4H-II with truncated alpha subunit (C-P4H-II delta281) Deposited 2022-05-06	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 18–508（491 aa）	Not recorded	SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6；278 K；20% (w/v) PEG4000, 0.2 M lithium sulfate, 0.1 M MES, 3% methanol	Resolution 3.85 Å R-free 0.278
7ZSC Crystal structure of the heterodimeric human C-P4H-II with truncated alpha subunit (C-P4H-II delta281) Deposited 2022-05-06	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 18–508（491 aa）	Not recorded	SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6；278 K；20% (w/v) PEG4000, 0.2 M lithium sulfate, 0.1 M MES, 3% methanol	Resolution 3.85 Å R-free 0.278
8EOJ Microsomal triglyceride transfer protein Deposited 2022-10-03	Different construct Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–508（508 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.07 Å
8GDY Crystal structure of the human PDI first domain with 9 mutations Deposited 2023-03-06	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 18–137（120 aa）	Mutation：K31R, K42R, K57R, K65R, K69R, K71R, K114R, K130R, K131R	SCN THIOCYANATE ION × 1 EDO 1,2-ETHANEDIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions MICROBATCH；pH 6；277 K；0.1 M potassium thiocyanate, 0.1 M MES, and 24% (w/v) PEG 20k	Resolution 2.05 Å R-free 0.239
8GDY Crystal structure of the human PDI first domain with 9 mutations Deposited 2023-03-06	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain B 18–137（120 aa）	Mutation：K31R, K42R, K57R, K65R, K69R, K71R, K114R, K130R, K131R	SCN THIOCYANATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions MICROBATCH；pH 6；277 K；0.1 M potassium thiocyanate, 0.1 M MES, and 24% (w/v) PEG 20k	Resolution 2.05 Å R-free 0.239

13 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	PDIA1_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 2–492； UniProt 18–508 Author chain B； PDBConstruct 2–492； UniProt 18–508

Microsomal triglyceride transfer protein large subunit

Homo sapiens

UniProt P55157

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 × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain G； UniProt 19–894	Not recorded	Protein disulfide-isomerase × 1 （P07237） CA CALCIUM ION × 1 EDO 1,2-ETHANEDIOL × 11 PGE TRIETHYLENE GLYCOL × 1 SO4 SULFATE ION × 7 PEG DI(HYDROXYETHYL)ETHER × 2 PE5 3,6,9,12,15,18,21,24-OCTAOXAHEXACOSAN-1-OL × 1 TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 7.5；277 K；0.1 M Tris pH 8.25, 0.2 M Li2SO4, 32% v/v PEG 400, 2% Polypropylene glycol P425	Resolution 2.50 Å R-free 0.257
2	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain H； UniProt 19–894	Not recorded	Protein disulfide-isomerase × 1 （P07237） CA CALCIUM ION × 1 EDO 1,2-ETHANEDIOL × 8 PGE TRIETHYLENE GLYCOL × 5 SO4 SULFATE ION × 4 PEG DI(HYDROXYETHYL)ETHER × 7 PE5 3,6,9,12,15,18,21,24-OCTAOXAHEXACOSAN-1-OL × 1 PE4 2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 7.5；277 K；0.1 M Tris pH 8.25, 0.2 M Li2SO4, 32% v/v PEG 400, 2% Polypropylene glycol P425	Resolution 2.50 Å R-free 0.257

Other States of the Same Protein in the Database

Other PDB	Difference from Current Entry 6I7S	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
8EOJ Microsomal triglyceride transfer protein Deposited 2022-10-03	Different construct 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 1–894（894 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.07 Å

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

View Construct and Data Evidence

UniProt name	MTP_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain G； PDBConstruct 9–884； UniProt 19–894 Author chain H； PDBConstruct 9–884； UniProt 19–894

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	6i7s
Deposition date deposition_date	2018-11-17
Structure title title	Microsomal triglyceride transfer protein
Keywords keywords	Lipid transfer, protein complex, protein disulfide isomerase, LIPID TRANSPORT; LIPID TRANSPORT
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	59.44 Å
Radius of gyration Rg (electron density) rg_electron	59.93 Å
Forward intensity I(0) i0	1262180000.00
Molecular weight molecular_weight	301100.0 kDa
Excluded volume excluded_volume	378980 Å³
Envelope volume envelope_volume	592150 Å³
Hydration-shell volume shell_volume	87972 Å³
Envelope diameter envelope_diameter	212.8 Å
Shell Rg shell_rg	56.39 Å
Envelope Rg envelope_rg	58.08 Å
Shape Rg shape_rg	59.88 Å
Total Rg total_rg	60.01 Å
Total atoms total_atoms	21163
Residues n_residues	2648
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	215.9 Å
Rg (real space) rg_real	59.95 Å
Rg uncertainty (real space) rg_real_error	2.94 Å
I(0) (real space) i0_real	1.2620e+09
I(0) uncertainty (real space) i0_real_error	2.6730e+07
Rg (reciprocal space) rg_reciprocal	58.99 Å
I(0) (reciprocal space) i0_reciprocal	1260000000.0000
Solution quality estimate total_estimate	0.8269
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	66.4 Å
Skewness Skewness skewness	0.512
Kurtosis Kurtosis kurtosis	-0.260
Angular range angular_range	— – 0.1300 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	68970000.0000
Real-space data points n_real_points	27
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.744; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.966; Smooth: 0.548

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (11)

Entity 1 Entity 1 polymer

Description description	Protein disulfide-isomerase
Molecular weight formula_weight	55496.0 kDa
EC 编号 ec_number	5.3.4.1
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	21452

MDAPEEEDHVLVLRKSNFAEALAAHKYLLVEFYAPWCGHCKALAPEYAKAAGKLKAEGSEIRLAKVDATEESDLAQQYGVRGYPTIKFFRNGDTASPKEYTAGREADDIVNWLKKRTGPAATTLPDGAAAESLVESSEVAVIGFFKDVESDSAKQFLQAAEAIDDIPFGITSNSDVFSKYQLDKDGVVLFKKFDEGRNNFEGEVTKENLLDFIKHNQLPLVIEFTEQTAPKIFGGEIKTHILLFLPKSVSDYDGKLSNFKTAAESFKGKILFIFIDSDHTDNQRILEFFGLKKEECPAVRLITLEEEMTKYKPESEELTAERITEFCHRFLEGKIKPHLMSQELPEDWDKQPVKVLVGKNFEDVAFDEKKNVFVEFYAPWCGHCKQLAPIWDKLGETYKDHENIVIAKMDSTANEVEAVKVHSFPTLKFFPASADRTVIDYNGERTLDGFKKFLESGGQDGAGDDDDLEDLEEAEEPDMEEDDDQKAVKDEL

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 K-12

Entity 2 Entity 2 polymer

Description description	Microsomal triglyceride transfer protein large subunit
Molecular weight formula_weight	98605.0 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

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

MHHHHHHMVKGHTTGLSLNNDRLYKLTYSTEVLLDRGKGKLQDSVGYRISSNVDVALLWRNPDGDDDQLIQITMKDVNVENVNQQRGEKSIFKGKSPSKIMGKENLEALQRPTLLHLIHGKVKEFYSYQNEAVAIENIKRGLASLFQTQLSSGTTNEVDISGNCKVTYQAHQDKVIKIKALDSCKIARSGFTTPNQVLGVSSKATSVTTYKIEDSFVIAVLAEETHNFGLNFLQTIKGKIVSKQKLELKTTEAGPRLMSGKQAAAIIKAVDSKYTAIPIVGQVFQSHCKGCPSLSELWRSTRKYLQPDNLSKAEAVRNFLAFIQHLRTAKKEEILQILKMENKEVLPQLVDAVTSAQTSDSLEAILDFLDFKSDSSIILQERFLYACGFASHPNEELLRALISKFKGSIGSSDIRETVMIITGTLVRKLCQNEGCKLKAVVEAKKLILGGLEKAEKKEDTRMYLLALKNALLPEGIPSLLKYAEAGEGPISHLATTALQRYDLPFITDEVKKTLNRIYHQNRKVHEKTVRTAAAAIILNNNPSYMDVKNILLSIGELPQEMNKYMLAIVQDILRFEMPASKIVRRVLKEMVAHNYDRFSRSGSSSAYTGYIERSPRSASTYSLDILYSGSGILRRSNLNIFQYIGKAGLHGSQVVIEAQGLEALIAATPDEGEENLDSYAGMSAILFDVQLRPVTFFNGYSDLMSKMLSASGDPISVVKGLILLIDHSQELQLQSGLKANIEVQGGLAIDISGAMEFSLWYRESKTRVKNRVTVVITTDITVDSSFVKAGLETSTETEAGLEFISTVQFSQYPFLVCMQMDKDEAPFRQFEKKYERLSTGRGYVSQKRKESVLAGCEFPLHQENSEMCKVVFAPQPDSTSSGWF

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 K-12

Entity 3 Entity 3 non-polymer

Description description	CALCIUM ION
Molecular weight formula_weight	40.1 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 4 Entity 4 non-polymer

Description description	1,2-ETHANEDIOL
Molecular weight formula_weight	62.1 kDa
Source method src_method	syn
Copy count entity_count	19

Entity 5 Entity 5 non-polymer

Description description	TRIETHYLENE GLYCOL
Molecular weight formula_weight	150.2 kDa
Source method src_method	syn
Copy count entity_count	6

Entity 6 Entity 6 non-polymer

Description description	SULFATE ION
Molecular weight formula_weight	96.1 kDa
Source method src_method	syn
Copy count entity_count	11

Entity 7 Entity 7 non-polymer

Description description	DI(HYDROXYETHYL)ETHER
Molecular weight formula_weight	106.1 kDa
Source method src_method	syn
Copy count entity_count	9

Entity 8 Entity 8 non-polymer

Description description	3,6,9,12,15,18,21,24-OCTAOXAHEXACOSAN-1-OL
Molecular weight formula_weight	398.5 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 9 Entity 9 non-polymer

Description description	2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL
Molecular weight formula_weight	122.1 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 10 Entity 10 non-polymer

Description description	2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL
Molecular weight formula_weight	354.4 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 11 Entity 11 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	222

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7. Fold Classification (SCOP + CATH) 10 domains

CATH v4.4 (10 domains)

Domain ID domain_id	6i7sA01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	30 — Glutaredoxin
Homologous superfamily homologous superfamily	10 — Glutaredoxin

Domain ID domain_id	6i7sA02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	30 — Glutaredoxin
Homologous superfamily homologous superfamily	10 — Glutaredoxin

Domain ID domain_id	6i7sA03
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	30 — Glutaredoxin
Homologous superfamily homologous superfamily	10 — Glutaredoxin

Domain ID domain_id	6i7sA04
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	30 — Glutaredoxin
Homologous superfamily homologous superfamily	10 — Glutaredoxin

Domain ID domain_id	6i7sB01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	30 — Glutaredoxin
Homologous superfamily homologous superfamily	10 — Glutaredoxin

Domain ID domain_id	6i7sB02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	30 — Glutaredoxin
Homologous superfamily homologous superfamily	10 — Glutaredoxin

Domain ID domain_id	6i7sB03
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	30 — Glutaredoxin
Homologous superfamily homologous superfamily	10 — Glutaredoxin

Domain ID domain_id	6i7sB04
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	30 — Glutaredoxin
Homologous superfamily homologous superfamily	10 — Glutaredoxin

Domain ID domain_id	6i7sG01
Class class	2 — Mainly Beta
Architecture architecture	30 — Roll
Topology topology	230 — Lipovitellin-phosvitin complex; beta-sheet shell regions
Homologous superfamily homologous superfamily	10 — Lipovitellin; beta-sheet shell regions, chain A

Domain ID domain_id	6i7sH01
Class class	2 — Mainly Beta
Architecture architecture	30 — Roll
Topology topology	230 — Lipovitellin-phosvitin complex; beta-sheet shell regions
Homologous superfamily homologous superfamily	10 — Lipovitellin; beta-sheet shell regions, chain A

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8. Citations (1)

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Unit-cell length a length_a	77.537 Å
Unit-cell length b length_b	105.595 Å
Unit-cell length c length_c	112.269 Å
Unit-cell angle α angle_alpha	89.81 °
Unit-cell angle β angle_beta	76.95 °
Unit-cell angle γ angle_gamma	74.24 °
Molecules per unit cell Z z_pdb	2

Space group space_group	P 1
Space-group number int_tables_number	1
Crystal system crystal_system	—

Resolution resolution	2.500 Å
Low-resolution limit resolution_low	49.350 Å
R factor r_factor	0.2071
R_work r_work	0.2045
R_free r_free	0.2571

fit	/app/data/saxs_computation/i7/6i7s/6i7s.fit
pddf	/app/data/pr_computation/i7/6i7s/6i7s.pr.out
profile	/app/data/saxs_computation/i7/6i7s/6i7s.dat

Microsomal triglyceride transfer protein

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

Protein disulfide-isomerase

State in the Current Structure

Other States of the Same Protein in the Database

Microsomal triglyceride transfer protein large subunit

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 (11)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

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

Entity 11 Entity 11 water

7. Fold Classification (SCOP + CATH) 10 domains

CATH v4.4 (10 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)