SANWENYU

sanwenyu-logo

Sanwenyu provides users with information about comic entertainment, film, television, and animation industry.

#People #Financial #Website #More

SANWENYU

Industry:
Animation Comics News

Founded:
2015-06-03

Address:
Beijing, Beijing, China

Country:
China

Website Url:
http://www.3wyu.com

Total Employee:
1+

Status:
Active

Email Addresses:
[email protected]

Total Funding:
13 M CNY

Technology used in webpage:
IPhone / Mobile Compatible Domain Not Resolving Euro Japanese Yen


Current Employees Featured

not_available_image

Shiwei Zhan
Shiwei Zhan Founder @ Sanwenyu
Founder

Founder


not_available_image

Shiwei Zhan

Investors List

bilibili-inc_image

Bilibili

Bilibili investment in Series A - Sanwenyu

great-chiliocosm-capital_image

Great Chiliocosm Capital

Great Chiliocosm Capital investment in Series A - Sanwenyu

leyo-capital_image

Leyo Capital

Leyo Capital investment in Angel Round - Sanwenyu

Official Site Inspections

http://www.3wyu.com

Unable to get host informations!!!

Loading ...

More informations about "Sanwenyu"

3WUY: Crystal structure of Nit6803 - RCSB PDB

May 9, 2014 3WUY; PubMed Abstract: Nitrilases are enzymes widely expressed in prokaryotes and eukaryotes that utilize a Cysโ€“Gluโ€“Lys catalytic triad to hydrolyze non-peptide carbonโ€“nitrogen bonds. Nitrilase from Syechocystis sp. โ€ฆSee details»

Characterization of the Nit6803 nitrilase homolog from the โ€ฆ

Mar 1, 2021 Structural organization of the Nit1C gene cluster in P. fluorescens NCIMB 11764. ... 3WUY) which shares 64% amino acid sequence identity with Nit11764. The modeled three โ€ฆSee details»

Cryo-EM structure of bacterial nitrilase reveals insight into ...

A .gov website belongs to an official government organization in the United States. Secure .gov websites use HTTPS A lock ( Locked padlock icon ... (PDB 6I00) and Nit6803 (PDB 3WUY). โ€ฆSee details»

Functional metagenomics uncovers nitrile-hydrolysing enzymes in โ€ฆ

Mar 17, 2023 The protein structure (3WUY), which was identified from Synechocystis sp. PCC 6803 substr. Kazusa, comprises 349 amino acids and has a resolution of 3.10 Å. The other โ€ฆSee details»

3WUY: Crystal Structure Of Nit6803 - National Center for โ€ฆ

Madej T, Lanczycki CJ, Zhang D, Thiessen PA, Geer RC, Marchler-Bauer A, Bryant SH. " MMDB and VAST+: tracking structural similarities between macromolecular complexes. Nucleic Acids โ€ฆSee details»

wwPDB: 3WUY - Protein Data Bank

May 9, 2014 Links to more resources for 3WUY at: News & Announcements. Community Bulletin Board. Download Archive. RCSB PDB | PDBe | PDBj Instructions. Archive Snapshots. โ€ฆSee details»

3wuy - Proteopedia, life in 3D

3wuy. From Proteopedia. Jump to: navigation, search. proteopedia link proteopedia link Crystal structure of Nit6803. spin quality labels all models. PDB ID 3wuy. Drag the structure with the โ€ฆSee details»

3D View: 3WUY - RCSB PDB

3WUY: Crystal structure of Nit6803. You are using a web browser that we do not support. Our website will not work properly.See details»

PDB 3wuy structure summary โ€น Protein Data Bank in Europe โ€ฆ

Dec 31, 2014 PDBe โ€บ 3wuy. X-ray diffraction. 3.1Å resolution. Crystal structure of Nit6803. Released: 31 Dec 2014. DOI: 10.2210/pdb3wuy/pdb. Source organism: Synechocystis sp. โ€ฆSee details»

Experiment: 3WUY - RCSB PDB

3WUY. Crystal structure of Nit6803. X-RAY DIFFRACTION. Starting Model(s) Initial Refinement Model(s) Type Source Accession Code Details; experimental model: Other: Structure โ€ฆSee details»

Frontiers | Functional metagenomics uncovers nitrile-hydrolysing ...

Mar 16, 2023 The area of the active site for 3WUY, 3IW3, and 3IVZ was 983.426 Å2, 61.447 Å2, and 188.905 Å2 and the volume was 1,129.287 Å3, 31.456 Å3, and 60.553 Å3, respectively. โ€ฆSee details»

Cryo-EM and directed evolution reveal how - Nature

Jul 17, 2019 Here we present what we believe to be the first close-to-atomic structure of a full-length active helical NIT (EC 3.5.5.1) using cryo-electron microscopy at a resolution of 3.4 Å.See details»

Genetic and Functional Diversity of Nitrilases in Agaricomycotina

Nov 28, 2019 The search revealed that all these NLases had the highest identities (30โ€“32%) to the NLase from Synechocystis sp. (3wuy) . In addition, NitTv1 had a 26% identity to an โ€ฆSee details»

Substrate specificity of plant nitrilase complexes is affected by โ€ฆ

Nov 2, 2018 Substrate specificity is one of the hallmarks of enzymes, the catalysts of the living cell. Understanding the principles of substrate recognition is an important step towards โ€ฆSee details»

Engineering of a nitrilase through consensus sequence analysis โ€ฆ

Jun 1, 2022 The model was based on the crystal structure of nitrilase Nit6803 from Syechocystis sp. PCC6803 (PDB: 3WUY). The catalytic triad E48/K130/C164 and mutation โ€ฆSee details»

Phe-140 Determines the Catalytic Efficiency of Arylacetonitrilase โ€ฆ

Oct 23, 2020 BLAST analysis using the protein database (PDB) revealed a considerable sequence identity (36%, 110/303) between NitAF and the protein Nit6803 (PDB accession โ€ฆSee details»

Cryo-EM structure of bacterial nitrilase reveals insight into ...

Jun 1, 2024 A) Structural comparison between Nitฮ”C39, AtNit4 (PDB 6I00) and Nit6803 (PDB 3WUY). An overall monomeric fold of the four enzymes, the backbone is colored from blue โ€ฆSee details»

Switching the secondary and natural activity of Nitrilase from

May 7, 2021 The three-dimensional structure model of Nit72W was generated using Modeller 9.19 with Nit6803 (Protein Data Bank: 3WUY) as the template with a sequence identity of 32% โ€ฆSee details»

1D PFV: 3WUY - RCSB PDB

As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon standards. The RCSB PDB also provides a variety of tools and resources. Users โ€ฆSee details»

Enhanced catalytic efficiency of nitrilase from Acidovorax facilis โ€ฆ

Nov 1, 2016 Since the nitrilase from Syechocystis sp. PCC6803 (PDB accession No. 3WUY) shared the highest sequence similarity (35%) with NitA, its crystal structure was used for โ€ฆSee details»

linkstock.net © 2022. All rights reserved