2WEO

Thermodynamic Optimisation of Carbonic Anhydrase Fragment Inhibitors

PDB DOI: https://doi.org/10.2210/pdb2WEO/pdb

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

Deposited: 2009-04-01 Released: 2009-11-10
Deposition Author(s): Scott, A.D., Phillips, C., Alex, A., Bent, A., O'Brien, R., Damian, L., Jones, L.H.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 1.40 Å
R-Value Free: 0.185
R-Value Work: 0.167
R-Value Observed: 0.167

wwPDB Validation 3D Report Full Report

Ligand Structure Quality Assessment

This is version 1.3 of the entry. See complete history.

Literature

Thermodynamic Optimisation in Drug Discovery: A Case Study Using Carbonic Anhydrase Inhibitors.

Scott, A.D., Phillips, C., Alex, A., Flocco, M., Bent, A., Randall, A., O'Brien, R., Damian, L., Jones, L.H.

(2009) ChemMedChem 4: 1985

PubMed: 19882701 Search on PubMed
DOI: https://doi.org/10.1002/cmdc.200900386
Primary Citation of Related Structures:
2WEG, 2WEH, 2WEJ, 2WEO

Organizational Affiliation

Pfizer Global Research & Development, Sandwich Laboratories, Ramsgate Road, Sandwich, Kent CT13 9NU., UK. [email protected]

Macromolecule Content

Total Structure Weight: 29.57 kDa
Atom Count: 2,287
Modelled Residue Count: 257
Deposited Residue Count: 259
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 2	A	259	Homo sapiens	Mutation(s): 0 EC: 4.2.1.1 (PDB Primary Data), 4.2.1.69 (UniProt)
UniProt & NIH Common Fund Data Resources
Find proteins for P00918 (Homo sapiens) Explore P00918 Go to UniProtKB: P00918
PHAROS: P00918 GTEx: ENSG00000104267
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	P00918
Sequence Annotations Expand
Reference Sequence

Small Molecules

Ligands 4 Unique
ID	Chains	Name / Formula / InChI Key	2D Diagram	3D Interactions
FBW Query on FBW Download Ideal Coordinates CCD File SDF format, chain C [auth A] MOL2 format, chain C [auth A] mmCIF format, chain C [auth A]	C [auth A]	3-fluorobenzenesulfonamide C₆ H₆ F N O₂ S CRINBBOGNYCAOV-UHFFFAOYSA-N		Interactions Focus chain C [auth A] Interactions & Density Focus chain C [auth A]
GOL Query on GOL Download Ideal Coordinates CCD File SDF format, chain D [auth A] MOL2 format, chain D [auth A] mmCIF format, chain D [auth A]	D [auth A]	GLYCEROL C₃ H₈ O₃ PEDCQBHIVMGVHV-UHFFFAOYSA-N		Interactions Focus chain D [auth A] Interactions & Density Focus chain D [auth A]
DMS Query on DMS Download Ideal Coordinates CCD File SDF format, chain E [auth A] MOL2 format, chain E [auth A] mmCIF format, chain E [auth A]	E [auth A]	DIMETHYL SULFOXIDE C₂ H₆ O S IAZDPXIOMUYVGZ-UHFFFAOYSA-N		Interactions Focus chain E [auth A] Interactions & Density Focus chain E [auth A]
ZN Query on ZN Download Ideal Coordinates CCD File SDF format, chain B [auth A] MOL2 format, chain B [auth A] mmCIF format, chain B [auth A]	B [auth A]	ZINC ION Zn PTFCDOFLOPIGGS-UHFFFAOYSA-N		Interactions Focus chain B [auth A] Interactions & Density Focus chain B [auth A]

Binding Affinity Annotations
ID	Source	Binding Affinity
FBW	PDBBind: 2WEO	Kd: 118 (nM) from 1 assay(s)

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 1.40 Å
R-Value Free: 0.185
R-Value Work: 0.167
R-Value Observed: 0.167
Space Group: P 1 2₁ 1

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 42.511	α = 90
b = 41.291	β = 109.5
c = 74.008	γ = 90

Software Package:

Software Name	Purpose
REFMAC	refinement

Structure Validation

View Full Validation Report

Ligand Structure Quality Assessment

Entry History

Deposition Data

Released Date: 2009-11-10

Deposition Author(s):

Revision History (Full details and data files)

Version 1.0: 2009-11-10
Type: Initial release
Version 1.1: 2011-06-09
Changes: Version format compliance
Version 1.2: 2011-07-13
Changes: Version format compliance
Version 1.3: 2024-05-08
Changes: Data collection, Database references, Derived calculations, Other

Prepare Data

Validate Data

Deposit Data

Help and Resources

2WEO

Thermodynamic Optimisation of Carbonic Anhydrase Fragment Inhibitors

Thermodynamic Optimisation in Drug Discovery: A Case Study Using Carbonic Anhydrase Inhibitors.

Entity ID: 1

UniProt & NIH Common Fund Data Resources

Entity Groups

Sequence Annotations

Expand

Experimental Data

Structure Validation

Ligand Structure Quality Assessment

Deposition Data

Revision History (Full details and data files)