3d protein structures Search Results


3d structures of the n-terminal domain of the matrix protein vp40  (AUTODOCK GmbH)
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AUTODOCK GmbH 3d structures of the n-terminal domain of the matrix protein vp40
3d Structures Of The N Terminal Domain Of The Matrix Protein Vp40, supplied by AUTODOCK GmbH, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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data from 3d structures of membrane proteins  (HighRes Biosolutions)
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HighRes Biosolutions data from 3d structures of membrane proteins
Data From 3d Structures Of Membrane Proteins, supplied by HighRes Biosolutions, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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informatics involving protein 3-d structures relevant to drug design  (Inpharmatica)
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Inpharmatica informatics involving protein 3-d structures relevant to drug design
Informatics Involving Protein 3 D Structures Relevant To Drug Design, supplied by Inpharmatica, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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3d protein structures  (SourceForge net)
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SourceForge net 3d protein structures
(A) Left: IST density of IRs on the <t>3D</t> <t>protein</t> structures of AP-1. ISTs obtained as prey in selections using FOS and JUN were mapped onto the 3D structure of AP-1 (PDB: 1A02, chain F and J; . Right: Contact regions of AP-1. All amino acids of one protein within 4.0 Å of the other protein are colored blue. IST densities are ranked and colored on a scale of 1 to >5 according to the number of ISTs at each amino acid position. (B) Left: MAX interacting regions in FTH1. Twenty-four ISTs derived from FTH1, obtained using MAX as bait, were mapped onto the 3D structure of FTH1 (PDB:1FHA; ). Right: Pull-down assay to evaluate the MAX/FTH interaction. ‘IR’ and ‘full’ correspond to the assays performed with the IR (region: 124.176) and full-length FTH, respectively, as bait. Full-length MAX was used as prey. (C) Left: SMAD2 interacting regions in RHOA. An IST derived from RHOA, obtained using SMAD2 as bait, was mapped onto the 3-D structure of RHOA (PDB: 1OW3, chain B; ). Right: Pull-down assay to evaluate the SMAD2/RHOA interaction. ‘IR’ and ‘full’ correspond to the assays performed with the IR (region: 38..63) and full-length RHOA, respectively, as bait. The (522..1401) region of SMAD2 was used as prey.
3d Protein Structures, supplied by SourceForge net, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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3d protein structures - by Bioz Stars, 2026-07
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3d structures of the sars-cov-1 spike protein  (BioNTech)
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BioNTech 3d structures of the sars-cov-1 spike protein

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predictive 3d protein structures  (Lawrence Livermore National Security LLC)
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Lawrence Livermore National Security LLC predictive 3d protein structures

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predictive 3d protein structures - by Bioz Stars, 2026-07
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3d protein-ligand complex structure visualization  (Schrodinger LLC)
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3d structure of jun protein docked with atorvastatin by autodock vina  (AUTODOCK GmbH)
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AUTODOCK GmbH 3d structure of jun protein docked with atorvastatin by autodock vina

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3d structure of the final bentec fusion protein  (Bentec Medical Inc)
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3d protein structure images of sblpmo9a and b  (Schrodinger LLC)
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Schrodinger LLC 3d protein structure images of sblpmo9a and b

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3d structures of the above-mentioned receptor proteins  (Schrodinger LLC)
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Schrodinger LLC 3d structures of the above-mentioned receptor proteins

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reference proteins 3d structures  (Databank Inc)
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Image Search Results


(A) Left: IST density of IRs on the 3D protein structures of AP-1. ISTs obtained as prey in selections using FOS and JUN were mapped onto the 3D structure of AP-1 (PDB: 1A02, chain F and J; . Right: Contact regions of AP-1. All amino acids of one protein within 4.0 Å of the other protein are colored blue. IST densities are ranked and colored on a scale of 1 to >5 according to the number of ISTs at each amino acid position. (B) Left: MAX interacting regions in FTH1. Twenty-four ISTs derived from FTH1, obtained using MAX as bait, were mapped onto the 3D structure of FTH1 (PDB:1FHA; ). Right: Pull-down assay to evaluate the MAX/FTH interaction. ‘IR’ and ‘full’ correspond to the assays performed with the IR (region: 124.176) and full-length FTH, respectively, as bait. Full-length MAX was used as prey. (C) Left: SMAD2 interacting regions in RHOA. An IST derived from RHOA, obtained using SMAD2 as bait, was mapped onto the 3-D structure of RHOA (PDB: 1OW3, chain B; ). Right: Pull-down assay to evaluate the SMAD2/RHOA interaction. ‘IR’ and ‘full’ correspond to the assays performed with the IR (region: 38..63) and full-length RHOA, respectively, as bait. The (522..1401) region of SMAD2 was used as prey.

Journal: PLoS ONE

Article Title: A Comprehensive Resource of Interacting Protein Regions for Refining Human Transcription Factor Networks

doi: 10.1371/journal.pone.0009289

Figure Lengend Snippet: (A) Left: IST density of IRs on the 3D protein structures of AP-1. ISTs obtained as prey in selections using FOS and JUN were mapped onto the 3D structure of AP-1 (PDB: 1A02, chain F and J; . Right: Contact regions of AP-1. All amino acids of one protein within 4.0 Å of the other protein are colored blue. IST densities are ranked and colored on a scale of 1 to >5 according to the number of ISTs at each amino acid position. (B) Left: MAX interacting regions in FTH1. Twenty-four ISTs derived from FTH1, obtained using MAX as bait, were mapped onto the 3D structure of FTH1 (PDB:1FHA; ). Right: Pull-down assay to evaluate the MAX/FTH interaction. ‘IR’ and ‘full’ correspond to the assays performed with the IR (region: 124.176) and full-length FTH, respectively, as bait. Full-length MAX was used as prey. (C) Left: SMAD2 interacting regions in RHOA. An IST derived from RHOA, obtained using SMAD2 as bait, was mapped onto the 3-D structure of RHOA (PDB: 1OW3, chain B; ). Right: Pull-down assay to evaluate the SMAD2/RHOA interaction. ‘IR’ and ‘full’ correspond to the assays performed with the IR (region: 38..63) and full-length RHOA, respectively, as bait. The (522..1401) region of SMAD2 was used as prey.

Article Snippet: All 3D protein structures presented in this paper were created using PyMol ( http://pymol.sourceforge.net ).

Techniques: Derivative Assay, Pull Down Assay

Journal: Structure (London, England : 1993)

Article Title: RCSB Protein Data Bank resources for structure-facilitated design of mRNA vaccines for existing and emerging viral pathogens

doi: 10.1016/j.str.2021.10.008

Figure Lengend Snippet:

Article Snippet: During the design phase, researchers at both Pfizer-BioNTech and Moderna had open access to a total of 18 3D structures of the extracellular portion of the SARS-CoV-1 spike protein (first PDB: 5x5b , publicly released 5/3/2017; ).

Techniques: Software