BindingDB Entry 50046191: Cloning, characterization and anion inhibition studies of a new¿-carbonic anhydrase from the Antarctic bacterium Pseudoalteromonas haloplanktis.

Small molecule binding data for protein Carbonic anhydrase, Carbonic anhydrase 2, and Gamma-carbonic anhydrase, Uniprot P00915, P00918, and P40881

Bibliographic Details
Main Author: BindingDB
Format: Dataset
Language:English
Published: BindingDB 2016
Subjects:
Carbonic anhydrase, Carbonic anhydrase 2, and Gamma-carbonic anhydrase, Istituto di Bioscienze e Biorisorse, Affinity
Antarctic
The Antarctic
Antarc*
Online Access:https://dx.doi.org/10.7270/q2jd4zj0
https://www.bindingdb.org/entry/50046191
id ftdatacite:10.7270/q2jd4zj0
record_format openpolar
spelling ftdatacite:10.7270/q2jd4zj0 2023-05-15T13:52:41+02:00 BindingDB Entry 50046191: Cloning, characterization and anion inhibition studies of a new¿-carbonic anhydrase from the Antarctic bacterium Pseudoalteromonas haloplanktis. BindingDB 2016 https://dx.doi.org/10.7270/q2jd4zj0 https://www.bindingdb.org/entry/50046191 en eng BindingDB https://www.ebi.ac.uk/chembl/ https://www.ebi.ac.uk/chembl/ https://dx.doi.org/10.1016/j.bmc.2015.06.021 Attribution 3.0 United States Carbonic anhydrase, Carbonic anhydrase 2, and Gamma-carbonic anhydrase, Istituto di Bioscienze e Biorisorse, Affinity Protein-ligand binding data dataset Dataset 2016 ftdatacite https://doi.org/10.7270/q2jd4zj0 https://doi.org/10.1016/j.bmc.2015.06.021 2021-11-05T12:55:41Z Small molecule binding data for protein Carbonic anhydrase, Carbonic anhydrase 2, and Gamma-carbonic anhydrase, Uniprot P00915, P00918, and P40881 Dataset Antarc* Antarctic DataCite Metadata Store (German National Library of Science and Technology) Antarctic The Antarctic
institution Open Polar
collection DataCite Metadata Store (German National Library of Science and Technology)
op_collection_id ftdatacite
language English
topic Carbonic anhydrase, Carbonic anhydrase 2, and Gamma-carbonic anhydrase, Istituto di Bioscienze e Biorisorse, Affinity
spellingShingle Carbonic anhydrase, Carbonic anhydrase 2, and Gamma-carbonic anhydrase, Istituto di Bioscienze e Biorisorse, Affinity
BindingDB
BindingDB Entry 50046191: Cloning, characterization and anion inhibition studies of a new¿-carbonic anhydrase from the Antarctic bacterium Pseudoalteromonas haloplanktis.
topic_facet Carbonic anhydrase, Carbonic anhydrase 2, and Gamma-carbonic anhydrase, Istituto di Bioscienze e Biorisorse, Affinity
description Small molecule binding data for protein Carbonic anhydrase, Carbonic anhydrase 2, and Gamma-carbonic anhydrase, Uniprot P00915, P00918, and P40881
format Dataset
author BindingDB
author_facet BindingDB
author_sort BindingDB
title BindingDB Entry 50046191: Cloning, characterization and anion inhibition studies of a new¿-carbonic anhydrase from the Antarctic bacterium Pseudoalteromonas haloplanktis.
title_short BindingDB Entry 50046191: Cloning, characterization and anion inhibition studies of a new¿-carbonic anhydrase from the Antarctic bacterium Pseudoalteromonas haloplanktis.
title_full BindingDB Entry 50046191: Cloning, characterization and anion inhibition studies of a new¿-carbonic anhydrase from the Antarctic bacterium Pseudoalteromonas haloplanktis.
title_fullStr BindingDB Entry 50046191: Cloning, characterization and anion inhibition studies of a new¿-carbonic anhydrase from the Antarctic bacterium Pseudoalteromonas haloplanktis.
title_full_unstemmed BindingDB Entry 50046191: Cloning, characterization and anion inhibition studies of a new¿-carbonic anhydrase from the Antarctic bacterium Pseudoalteromonas haloplanktis.
title_sort bindingdb entry 50046191: cloning, characterization and anion inhibition studies of a new¿-carbonic anhydrase from the antarctic bacterium pseudoalteromonas haloplanktis.
publisher BindingDB
publishDate 2016
url https://dx.doi.org/10.7270/q2jd4zj0
https://www.bindingdb.org/entry/50046191
geographic Antarctic
The Antarctic
geographic_facet Antarctic
The Antarctic
genre Antarc*
Antarctic
genre_facet Antarc*
Antarctic
op_relation https://www.ebi.ac.uk/chembl/
https://www.ebi.ac.uk/chembl/
https://dx.doi.org/10.1016/j.bmc.2015.06.021
op_rights Attribution 3.0 United States
op_doi https://doi.org/10.7270/q2jd4zj0
https://doi.org/10.1016/j.bmc.2015.06.021
_version_ 1766257104438427648

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