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7k5w

Cryo-EM structure of heterologous protein complex loaded Thermotoga maritima encapsulin capsid

Method: ELECTRON MICROSCOPY Dmax: 82.8 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Maritimacin

Thermotoga maritima

UniProt Q9WZP2

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 × 60 PDB declaration: 60-meric（60） Consistent with protein copy count Chain A； UniProt 1–265 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 2.87 Å
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain A； UniProt 1–265 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 2.87 Å
3 Protein homooligomer Homooligomer Protein × 5 PDB declaration: pentameric（5） Consistent with protein copy count Chain A； UniProt 1–265 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 2.87 Å
4 Protein homooligomer Homooligomer Protein × 6 PDB declaration: hexameric（6） Consistent with protein copy count Chain A； UniProt 1–265 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 2.87 Å
5 Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain A； UniProt 1–265 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 2.87 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 7K5W Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
3DKT Crystal structure of Thermotoga maritima encapsulin Deposited 2008-06-26 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 120 PDB declaration: 120-meric
Chain A 1–265（265 aa）
Chain B 1–265（265 aa）
Chain C 1–265（265 aa）
Chain D 1–265（265 aa）
Chain E 1–265（265 aa）
Chain F 1–265（265 aa）
Chain G 1–265（265 aa）
Chain H 1–265（265 aa）
Chain I 1–265（265 aa）
Chain J 1–265（265 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.1；292 K；0.1M citrate, 21.5% MPD (v/v), 0.25M ammonium acetate, pH5.1, VAPOR DIFFUSION, SITTING DROP, temperature 292K
Resolution 3.10 Å R-free 0.239
6WKV Cryo-EM structure of engineered variant of the Encapsulin from Thermotoga maritima (TmE) Deposited 2020-04-17 Different construct Different mutation/modification Different ligand/ion Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 60 PDB declaration: 60-meric
Chain 0 1–265（265 aa）
Chain 1 1–265（265 aa）
Chain 2 1–265（265 aa）
Chain 3 1–265（265 aa）
Chain 4 1–265（265 aa）
Chain 5 1–265（265 aa）
Chain 6 1–265（265 aa）
Chain 7 1–265（265 aa）
Chain 8 1–265（265 aa）
Chain 9 1–265（265 aa）
Chain A 1–265（265 aa）
Chain B 1–265（265 aa）
Chain C 1–265（265 aa）
Chain D 1–265（265 aa）
Chain E 1–265（265 aa）
Chain F 1–265（265 aa）
Chain G 1–265（265 aa）
Chain H 1–265（265 aa）
Chain I 1–265（265 aa）
Chain J 1–265（265 aa）
Chain K 1–265（265 aa）
Chain L 1–265（265 aa）
Chain M 1–265（265 aa）
Chain N 1–265（265 aa）
Chain O 1–265（265 aa）
Chain P 1–265（265 aa）
Chain Q 1–265（265 aa）
Chain R 1–265（265 aa）
Chain S 1–265（265 aa）
Chain T 1–265（265 aa）
Chain U 1–265（265 aa）
Chain V 1–265（265 aa）
Chain W 1–265（265 aa）
Chain X 1–265（265 aa）
Chain Y 1–265（265 aa）
Chain Z 1–265（265 aa）
Chain a 1–265（265 aa）
Chain b 1–265（265 aa）
Chain c 1–265（265 aa）
Chain d 1–265（265 aa）
Chain e 1–265（265 aa）
Chain f 1–265（265 aa）
Chain g 1–265（265 aa）
Chain h 1–265（265 aa）
Chain i 1–265（265 aa）
Chain j 1–265（265 aa）
Chain k 1–265（265 aa）
Chain l 1–265（265 aa）
Chain m 1–265（265 aa）
Chain n 1–265（265 aa）
Chain o 1–265（265 aa）
Chain p 1–265（265 aa）
Chain q 1–265（265 aa）
Chain r 1–265（265 aa）
Chain s 1–265（265 aa）
Chain t 1–265（265 aa）
Chain u 1–265（265 aa）
Chain v 1–265（265 aa）
Chain w 1–265（265 aa）
Chain x 1–265（265 aa）
Not recorded FMN FLAVIN MONONUCLEOTIDE × 60 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.99 Å
7KQ5 Cryo-EM structure of a thermostable encapsulin from T. maritima Deposited 2020-11-13 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 60 PDB declaration: 60-meric
Chain A 1–265（265 aa）
Not recorded FMN FLAVIN MONONUCLEOTIDE × 60 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen PROPANE；3 ul sample applied to the carbon side of the grid and blotted for 4s before plunging.
Resolution 2.00 Å
7KQ5 Cryo-EM structure of a thermostable encapsulin from T. maritima Deposited 2020-11-13 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–265（265 aa）
Not recorded FMN FLAVIN MONONUCLEOTIDE × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen PROPANE；3 ul sample applied to the carbon side of the grid and blotted for 4s before plunging.
Resolution 2.00 Å
7KQ5 Cryo-EM structure of a thermostable encapsulin from T. maritima Deposited 2020-11-13 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric
Chain A 1–265（265 aa）
Not recorded FMN FLAVIN MONONUCLEOTIDE × 5 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen PROPANE；3 ul sample applied to the carbon side of the grid and blotted for 4s before plunging.
Resolution 2.00 Å
7KQ5 Cryo-EM structure of a thermostable encapsulin from T. maritima Deposited 2020-11-13 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain A 1–265（265 aa）
Not recorded FMN FLAVIN MONONUCLEOTIDE × 6 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen PROPANE；3 ul sample applied to the carbon side of the grid and blotted for 4s before plunging.
Resolution 2.00 Å
7KQ5 Cryo-EM structure of a thermostable encapsulin from T. maritima Deposited 2020-11-13 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 5 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–265（265 aa）
Not recorded FMN FLAVIN MONONUCLEOTIDE × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen PROPANE；3 ul sample applied to the carbon side of the grid and blotted for 4s before plunging.
Resolution 2.00 Å
7LII Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S7D Deposited 2021-01-27 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 60 PDB declaration: 60-meric
Chain A 1–265（265 aa）
Mutation：K182D, E183D, Del(184-190) RBF RIBOFLAVIN × 60 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE；blot 4 seconds, force 20 immediately prior to plunging into ethane
Resolution 3.55 Å
7LII Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S7D Deposited 2021-01-27 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–265（265 aa）
Mutation：K182D, E183D, Del(184-190) RBF RIBOFLAVIN × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE；blot 4 seconds, force 20 immediately prior to plunging into ethane
Resolution 3.55 Å
7LII Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S7D Deposited 2021-01-27 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric
Chain A 1–265（265 aa）
Mutation：K182D, E183D, Del(184-190) RBF RIBOFLAVIN × 5 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE；blot 4 seconds, force 20 immediately prior to plunging into ethane
Resolution 3.55 Å
7LII Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S7D Deposited 2021-01-27 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain A 1–265（265 aa）
Mutation：K182D, E183D, Del(184-190) RBF RIBOFLAVIN × 6 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE；blot 4 seconds, force 20 immediately prior to plunging into ethane
Resolution 3.55 Å
7LII Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S7D Deposited 2021-01-27 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 5 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–265（265 aa）
Mutation：K182D, E183D, Del(184-190) RBF RIBOFLAVIN × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE；blot 4 seconds, force 20 immediately prior to plunging into ethane
Resolution 3.55 Å
7LIJ Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S1K Deposited 2021-01-27 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 60 PDB declaration: 60-meric
Chain A 1–265（265 aa）
Mutation：H187K RBF RIBOFLAVIN × 60 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE；blot 4 seconds, force 20 immediately prior to plunging into ethane
Resolution 2.84 Å
7LIJ Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S1K Deposited 2021-01-27 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–265（265 aa）
Mutation：H187K RBF RIBOFLAVIN × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE；blot 4 seconds, force 20 immediately prior to plunging into ethane
Resolution 2.84 Å
7LIJ Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S1K Deposited 2021-01-27 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric
Chain A 1–265（265 aa）
Mutation：H187K RBF RIBOFLAVIN × 5 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE；blot 4 seconds, force 20 immediately prior to plunging into ethane
Resolution 2.84 Å
7LIJ Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S1K Deposited 2021-01-27 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain A 1–265（265 aa）
Mutation：H187K RBF RIBOFLAVIN × 6 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE；blot 4 seconds, force 20 immediately prior to plunging into ethane
Resolution 2.84 Å
7LIJ Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S1K Deposited 2021-01-27 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 5 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–265（265 aa）
Mutation：H187K RBF RIBOFLAVIN × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE；blot 4 seconds, force 20 immediately prior to plunging into ethane
Resolution 2.84 Å
7LIK Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S1R Deposited 2021-01-27 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 60 PDB declaration: 60-meric
Chain A 1–265（265 aa）
Mutation：H187R RBF RIBOFLAVIN × 60 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE；blot 4 seconds, force 20 immediately prior to plunging into ethane
Resolution 2.91 Å
7LIK Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S1R Deposited 2021-01-27 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–265（265 aa）
Mutation：H187R RBF RIBOFLAVIN × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE；blot 4 seconds, force 20 immediately prior to plunging into ethane
Resolution 2.91 Å
7LIK Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S1R Deposited 2021-01-27 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric
Chain A 1–265（265 aa）
Mutation：H187R RBF RIBOFLAVIN × 5 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE；blot 4 seconds, force 20 immediately prior to plunging into ethane
Resolution 2.91 Å
7LIK Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S1R Deposited 2021-01-27 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain A 1–265（265 aa）
Mutation：H187R RBF RIBOFLAVIN × 6 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE；blot 4 seconds, force 20 immediately prior to plunging into ethane
Resolution 2.91 Å
7LIK Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S1R Deposited 2021-01-27 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 5 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–265（265 aa）
Mutation：H187R RBF RIBOFLAVIN × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE；blot 4 seconds, force 20 immediately prior to plunging into ethane
Resolution 2.91 Å
7LIL Thermotoga maritima Encapsulin Nanocompartment Pore Mutant SE3 Deposited 2021-01-27 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 60 PDB declaration: 60-meric
Chain A 1–265（265 aa）
Mutation：G186E,H187E,Y188E RBF RIBOFLAVIN × 60 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE；blot 4 seconds, force 20 immediately prior to plunging into ethane
Resolution 2.84 Å
7LIL Thermotoga maritima Encapsulin Nanocompartment Pore Mutant SE3 Deposited 2021-01-27 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–265（265 aa）
Mutation：G186E,H187E,Y188E RBF RIBOFLAVIN × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE；blot 4 seconds, force 20 immediately prior to plunging into ethane
Resolution 2.84 Å
7LIL Thermotoga maritima Encapsulin Nanocompartment Pore Mutant SE3 Deposited 2021-01-27 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric
Chain A 1–265（265 aa）
Mutation：G186E,H187E,Y188E RBF RIBOFLAVIN × 5 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE；blot 4 seconds, force 20 immediately prior to plunging into ethane
Resolution 2.84 Å
7LIL Thermotoga maritima Encapsulin Nanocompartment Pore Mutant SE3 Deposited 2021-01-27 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain A 1–265（265 aa）
Mutation：G186E,H187E,Y188E RBF RIBOFLAVIN × 6 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE；blot 4 seconds, force 20 immediately prior to plunging into ethane
Resolution 2.84 Å
7LIL Thermotoga maritima Encapsulin Nanocompartment Pore Mutant SE3 Deposited 2021-01-27 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 5 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–265（265 aa）
Mutation：G186E,H187E,Y188E RBF RIBOFLAVIN × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE；blot 4 seconds, force 20 immediately prior to plunging into ethane
Resolution 2.84 Å
7LIM Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S6E Deposited 2021-01-27 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 60 PDB declaration: 60-meric
Chain A 1–265（265 aa）
Mutation：Del(184-190) RBF RIBOFLAVIN × 60 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE；blot 4 seconds, force 20 immediately prior to plunging into ethane
Resolution 2.75 Å
7LIM Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S6E Deposited 2021-01-27 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–265（265 aa）
Mutation：Del(184-190) RBF RIBOFLAVIN × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE；blot 4 seconds, force 20 immediately prior to plunging into ethane
Resolution 2.75 Å
7LIM Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S6E Deposited 2021-01-27 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric
Chain A 1–265（265 aa）
Mutation：Del(184-190) RBF RIBOFLAVIN × 5 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE；blot 4 seconds, force 20 immediately prior to plunging into ethane
Resolution 2.75 Å
7LIM Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S6E Deposited 2021-01-27 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain A 1–265（265 aa）
Mutation：Del(184-190) RBF RIBOFLAVIN × 6 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE；blot 4 seconds, force 20 immediately prior to plunging into ethane
Resolution 2.75 Å
7LIM Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S6E Deposited 2021-01-27 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 5 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–265（265 aa）
Mutation：Del(184-190) RBF RIBOFLAVIN × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE；blot 4 seconds, force 20 immediately prior to plunging into ethane
Resolution 2.75 Å
7LIS Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S5D Deposited 2021-01-27 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 60 PDB declaration: 60-meric
Chain A 1–265（265 aa）
Mutation：E184D,P189D, Del(185-188) RBF RIBOFLAVIN × 60 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE；blot force 0, wait time 30 seconds
Resolution 2.96 Å
7LIS Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S5D Deposited 2021-01-27 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–265（265 aa）
Mutation：E184D,P189D, Del(185-188) RBF RIBOFLAVIN × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE；blot force 0, wait time 30 seconds
Resolution 2.96 Å
7LIS Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S5D Deposited 2021-01-27 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric
Chain A 1–265（265 aa）
Mutation：E184D,P189D, Del(185-188) RBF RIBOFLAVIN × 5 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE；blot force 0, wait time 30 seconds
Resolution 2.96 Å
7LIS Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S5D Deposited 2021-01-27 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain A 1–265（265 aa）
Mutation：E184D,P189D, Del(185-188) RBF RIBOFLAVIN × 6 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE；blot force 0, wait time 30 seconds
Resolution 2.96 Å
7LIS Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S5D Deposited 2021-01-27 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 5 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–265（265 aa）
Mutation：E184D,P189D, Del(185-188) RBF RIBOFLAVIN × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE；blot force 0, wait time 30 seconds
Resolution 2.96 Å
7LIT Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S7G Deposited 2021-01-27 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 60 PDB declaration: 60-meric
Chain A 1–265（265 aa）
Mutation：K182G, L190G, Del(182-189) RBF RIBOFLAVIN × 60 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE；blot force 0, wait time 30 seconds
Resolution 2.53 Å
7LIT Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S7G Deposited 2021-01-27 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–265（265 aa）
Mutation：K182G, L190G, Del(182-189) RBF RIBOFLAVIN × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE；blot force 0, wait time 30 seconds
Resolution 2.53 Å
7LIT Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S7G Deposited 2021-01-27 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric
Chain A 1–265（265 aa）
Mutation：K182G, L190G, Del(182-189) RBF RIBOFLAVIN × 5 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE；blot force 0, wait time 30 seconds
Resolution 2.53 Å
7LIT Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S7G Deposited 2021-01-27 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain A 1–265（265 aa）
Mutation：K182G, L190G, Del(182-189) RBF RIBOFLAVIN × 6 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE；blot force 0, wait time 30 seconds
Resolution 2.53 Å
7LIT Thermotoga maritima Encapsulin Nanocompartment Pore Mutant S7G Deposited 2021-01-27 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 5 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–265（265 aa）
Mutation：K182G, L190G, Del(182-189) RBF RIBOFLAVIN × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE；blot force 0, wait time 30 seconds
Resolution 2.53 Å
7MU1 Thermotoga maritima encapsulin shell Deposited 2021-05-14 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 60 PDB declaration: 60-meric
Chain A 1–264（264 aa）
Not recorded FMN FLAVIN MONONUCLEOTIDE × 60 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4；20 mM Tris-HCl, pH 7.4, 150 mM NaCl and 5 mM 2-mercaptoethanol
cryo-EM vitrification conditions Cryogen ETHANE-PROPANE；blot force
Resolution 3.30 Å
7MU1 Thermotoga maritima encapsulin shell Deposited 2021-05-14 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–264（264 aa）
Not recorded FMN FLAVIN MONONUCLEOTIDE × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4；20 mM Tris-HCl, pH 7.4, 150 mM NaCl and 5 mM 2-mercaptoethanol
cryo-EM vitrification conditions Cryogen ETHANE-PROPANE；blot force
Resolution 3.30 Å
7MU1 Thermotoga maritima encapsulin shell Deposited 2021-05-14 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric
Chain A 1–264（264 aa）
Not recorded FMN FLAVIN MONONUCLEOTIDE × 5 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4；20 mM Tris-HCl, pH 7.4, 150 mM NaCl and 5 mM 2-mercaptoethanol
cryo-EM vitrification conditions Cryogen ETHANE-PROPANE；blot force
Resolution 3.30 Å
7MU1 Thermotoga maritima encapsulin shell Deposited 2021-05-14 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain A 1–264（264 aa）
Not recorded FMN FLAVIN MONONUCLEOTIDE × 6 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4；20 mM Tris-HCl, pH 7.4, 150 mM NaCl and 5 mM 2-mercaptoethanol
cryo-EM vitrification conditions Cryogen ETHANE-PROPANE；blot force
Resolution 3.30 Å
7MU1 Thermotoga maritima encapsulin shell Deposited 2021-05-14 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 5 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–264（264 aa）
Not recorded FMN FLAVIN MONONUCLEOTIDE × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4；20 mM Tris-HCl, pH 7.4, 150 mM NaCl and 5 mM 2-mercaptoethanol
cryo-EM vitrification conditions Cryogen ETHANE-PROPANE；blot force
Resolution 3.30 Å
9Y8P Cryo-EM structure of Thermotoga maritima encapsulin shell Deposited 2025-09-11 Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 60 PDB declaration: 60-meric
Chain A 1–265（265 aa）
Chain AA 1–265（265 aa）
Chain AB 1–265（265 aa）
Chain B 1–265（265 aa）
Chain BA 1–265（265 aa）
Chain BB 1–265（265 aa）
Chain C 1–265（265 aa）
Chain CA 1–265（265 aa）
Chain CB 1–265（265 aa）
Chain D 1–265（265 aa）
Chain DA 1–265（265 aa）
Chain DB 1–265（265 aa）
Chain E 1–265（265 aa）
Chain EA 1–265（265 aa）
Chain EB 1–265（265 aa）
Chain F 1–265（265 aa）
Chain FA 1–265（265 aa）
Chain FB 1–265（265 aa）
Chain G 1–265（265 aa）
Chain GA 1–265（265 aa）
Chain GB 1–265（265 aa）
Chain H 1–265（265 aa）
Chain HA 1–265（265 aa）
Chain HB 1–265（265 aa）
Chain I 1–265（265 aa）
Chain IA 1–265（265 aa）
Chain J 1–265（265 aa）
Chain JA 1–265（265 aa）
Chain K 1–265（265 aa）
Chain KA 1–265（265 aa）
Chain L 1–265（265 aa）
Chain LA 1–265（265 aa）
Chain M 1–265（265 aa）
Chain MA 1–265（265 aa）
Chain N 1–265（265 aa）
Chain NA 1–265（265 aa）
Chain O 1–265（265 aa）
Chain OA 1–265（265 aa）
Chain P 1–265（265 aa）
Chain PA 1–265（265 aa）
Chain Q 1–265（265 aa）
Chain QA 1–265（265 aa）
Chain R 1–265（265 aa）
Chain RA 1–265（265 aa）
Chain S 1–265（265 aa）
Chain SA 1–265（265 aa）
Chain T 1–265（265 aa）
Chain TA 1–265（265 aa）
Chain U 1–265（265 aa）
Chain UA 1–265（265 aa）
Chain V 1–265（265 aa）
Chain VA 1–265（265 aa）
Chain W 1–265（265 aa）
Chain WA 1–265（265 aa）
Chain X 1–265（265 aa）
Chain XA 1–265（265 aa）
Chain Y 1–265（265 aa）
Chain YA 1–265（265 aa）
Chain Z 1–265（265 aa）
Chain ZA 1–265（265 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.80 Å

12 other PDB entries and 48 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MARIT_THEMA
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–265； UniProt 1–265

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

SAXS profile for 7k5w

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7k5w
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7k5w
Deposition date deposition_date2020-09-17
Structure title titleCryo-EM structure of heterologous protein complex loaded Thermotoga maritima encapsulin capsid
Keywords keywordsencapsulin, baculovirus expression system, cargo loading peptide, complex assembly, METAL BINDING PROTEIN, HYDROLASE; HYDROLASE
Experimental Method methodELECTRON MICROSCOPY
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier24.03 Å
Radius of gyration Rg (electron density) rg_electron23.13 Å
Forward intensity I(0) i015163700.00
Molecular weight molecular_weight30301.0 kDa
Excluded volume excluded_volume38341 ų
Envelope volume envelope_volume47069 ų
Hydration-shell volume shell_volume18515 ų
Envelope diameter envelope_diameter84.5 Å
Shell Rg shell_rg27.97 Å
Envelope Rg envelope_rg23.64 Å
Shape Rg shape_rg23.13 Å
Total Rg total_rg23.82 Å
Total atoms total_atoms2141
Residues n_residues264
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax82.8 Å
Rg (real space) rg_real24.12 Å
Rg uncertainty (real space) rg_real_error0.62 Å
I(0) (real space) i0_real1.5160e+07
I(0) uncertainty (real space) i0_real_error1.9290e+05
Rg (reciprocal space) rg_reciprocal24.10 Å
I(0) (reciprocal space) i0_reciprocal15160000.0000
Solution quality estimate total_estimate0.8574
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.0 Å
Skewness Skewness skewness0.361
Kurtosis Kurtosis kurtosis-0.520
Angular range angular_range— – 0.3300 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2851000.0000
Real-space data points n_real_points65
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.789; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.791; Smooth: 0.984
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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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8. Citations (1)

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9. Files and Curves (10)