9EP2 | pdb_00009ep2

Crystal structure of the complex of human carbonic anhydrase I with 4-sulfamoylphenyl 3-(p-tolylthio)propanoate

PDB DOI: https://doi.org/10.2210/pdb9EP2/pdb

Classification: LYASE
Organism(s): Homo sapiens
Expression System: Escherichia coli
Mutation(s): No

Deposited: 2024-03-16 Released: 2025-03-26
Deposition Author(s): Angeli, A., Ferraroni, M.
Funding Organization(s): Not funded

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 1.47 Å
R-Value Free:
0.209 (Depositor), 0.232 (DCC)
R-Value Work:
0.160 (Depositor), 0.181 (DCC)

Starting Model: experimental
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wwPDB Validation 3D Report Full Report

Ligand Structure Quality Assessment

This is version 1.1 of the entry. See complete history.

Literature

Thia- and Seleno-Michael Reactions for the Synthesis of Carbonic Anhydrases Inhibitors.

Angeli, A., Occhini, A., Renzi, G., Capperucci, A., Ferraroni, M., Tanini, D., Supuran, C.T.

(2024) ChemMedChem 19: e202400345-e202400345

PubMed: 39031732 Search on PubMed
DOI: https://doi.org/10.1002/cmdc.202400345
Primary Citation of Related Structures:
9EP2

PubMed Abstract:
Novel chalcogen-containing amides and esters bearing the benzenesulfonamide moiety have been synthesised upon nucleophilic conjugate addition of thiols and selenols to suitable electron-deficient alkenes. The activity of the synthesised compounds as Carbonic Anhydrases inhibitors has been investigated in vitro and the inhibition mechanism has been elucidated by X-rays studies.

Organizational Affiliation

NEUROFARBA Deptartment, Sezione di Scienze Farmaceutiche, University of Florence, Via Ugo Schiff 6, Sesto Fiorentino, 50019, Florence, Italy.

Macromolecule Content

Total Structure Weight: 58.76 kDa
Atom Count: 4,599
Modeled Residue Count: 516
Deposited Residue Count: 522
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
Carbonic anhydrase 1	A [auth AAA], B [auth BBB]	261	Homo sapiens	Mutation(s): 0 Gene Names: CA1 EC: 4.2.1.1 (PDB Primary Data), 4.2.1.69 (UniProt)
UniProt & NIH Common Fund Data Resources
Find proteins for P00915 (Homo sapiens) Explore P00915 Go to UniProtKB: P00915
PHAROS: P00915 GTEx: ENSG00000133742
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	P00915
Sequence Annotations Expand
Reference Sequence

Small Molecules

Ligands 3 Unique
ID	Chains	Name / Formula / InChI Key	2D Diagram	3D Interactions
A1H6C (Subject of Investigation/LOI) Query on A1H6C Download Ideal Coordinates CCD File SDF format, chain F [auth AAA] SDF format, chain H [auth BBB] MOL2 format, chain F [auth AAA] MOL2 format, chain H [auth BBB] mmCIF format, chain F [auth AAA] mmCIF format, chain H [auth BBB]	F [auth AAA], H [auth BBB]	(4-sulfamoylphenyl) 3-(4-methylphenyl)sulfanylpropanoate C₁₆ H₁₇ N O₄ S₂ AQONNBBQRNVHRO-UHFFFAOYSA-N		Interactions Focus chain F [auth AAA] Focus chain H [auth BBB] Interactions & Density Focus chain F [auth AAA] Focus chain H [auth BBB]
ZN Query on ZN Download Ideal Coordinates CCD File SDF format, chain E [auth AAA] SDF format, chain G [auth BBB] MOL2 format, chain E [auth AAA] MOL2 format, chain G [auth BBB] mmCIF format, chain E [auth AAA] mmCIF format, chain G [auth BBB]	E [auth AAA], G [auth BBB]	ZINC ION Zn PTFCDOFLOPIGGS-UHFFFAOYSA-N		Interactions Focus chain E [auth AAA] Focus chain G [auth BBB] Interactions & Density Focus chain E [auth AAA] Focus chain G [auth BBB]
ACT Query on ACT Download Ideal Coordinates CCD File SDF format, chain D [auth AAA] SDF format, chain C [auth AAA] MOL2 format, chain D [auth AAA] MOL2 format, chain C [auth AAA] mmCIF format, chain D [auth AAA] mmCIF format, chain C [auth AAA]	C [auth AAA], D [auth AAA]	ACETATE ION C₂ H₃ O₂ QTBSBXVTEAMEQO-UHFFFAOYSA-M		Interactions Focus chain C [auth AAA] Focus chain D [auth AAA] Interactions & Density Focus chain C [auth AAA] Focus chain D [auth AAA]