5L6K

Crystal Structure of Human Carbonic Anhydrase II in Complex with a Quinoline Oligoamide Foldamer


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.70 Å
  • R-Value Free: 0.181 
  • R-Value Work: 0.154 
  • R-Value Observed: 0.155 

wwPDB Validation   3D Report Full Report


Ligand Structure Quality Assessment 


This is version 3.1 of the entry. See complete history


Literature

Self-Assembled Protein-Aromatic Foldamer Complexes with 2:3 and 2:2:1 Stoichiometries.

Jewginski, M.Granier, T.Langlois d'Estaintot, B.Fischer, L.Mackereth, C.D.Huc, I.

(2017) J Am Chem Soc 139: 2928-2931

  • DOI: https://doi.org/10.1021/jacs.7b00184
  • Primary Citation of Related Structures:  
    5L3O, 5L6K, 5LVS

  • PubMed Abstract: 

    The promotion of protein dimerization using the aggregation properties of a protein ligand was explored and shown to produce complexes with unusual stoichiometries. Helical foldamer 2 was synthesized and bound to human carbonic anhydrase (HCA) using a nanomolar active site ligand. Crystal structures show that the hydrophobicity of 2 and interactions of its side chains lead to the formation of an HCA 2 -2 3 complex in which three helices of 2 are stacked, two of them being linked to an HCA molecule. The middle foldamer in the stack can be replaced by alternate sequences 3 or 5. Solution studies by CD and NMR confirm left-handedness of the helical foldamers as well as HCA dimerization.


  • Organizational Affiliation

    CBMN (UMR5248), Univ. Bordeaux, CNRS, IPB , Institut Européen de Chimie et Biologie, 2 rue Robert Escarpit, 33600 Pessac, France.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Carbonic anhydrase 2
A, B
260Homo sapiensMutation(s): 0 
Gene Names: CA2
EC: 4.2.1.1
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 Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP00918
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 10 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
6H0
Query on 6H0

Download Ideal Coordinates CCD File 
D [auth A],
W [auth B]
~{N}-[[3-(4-formamidobutoxy)phenyl]methyl]-4-sulfamoyl-benzamide
C19 H23 N3 O5 S
ASGCSQAUBAMMLK-UHFFFAOYSA-N
QVE
Query on QVE

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BA [auth B],
G [auth A],
I [auth A],
Z [auth B]
8-azanyl-4-(2-hydroxy-2-oxoethyloxy)quinoline-2-carboxylic acid
C12 H10 N2 O5
ISBWTKCQKHNORE-UHFFFAOYSA-N
QUK
Query on QUK

Download Ideal Coordinates CCD File 
AA [auth B],
E [auth A],
H [auth A],
X [auth B]
8-azanyl-4-(3-azanylpropoxy)quinoline-2-carboxylic acid
C13 H15 N3 O3
QGMHWPPZJKLYHR-UHFFFAOYSA-N
QUJ
Query on QUJ

Download Ideal Coordinates CCD File 
M [auth A],
Q [auth A],
R [auth B],
T [auth B]
8-azanyl-4-(2-methylpropoxy)quinoline-2-carboxylic acid
C14 H16 N2 O3
UQMUZAYVJKDBFB-UHFFFAOYSA-N
QVS
Query on QVS

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F [auth A],
N [auth A],
U [auth B],
Y [auth B]
8-azanyl-4-oxidanyl-quinoline-2-carboxylic acid
C10 H8 N2 O3
KZBXAHDVCSOKJO-UHFFFAOYSA-N
PG4
Query on PG4

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L [auth A],
S [auth B]
TETRAETHYLENE GLYCOL
C8 H18 O5
UWHCKJMYHZGTIT-UHFFFAOYSA-N
GOL
Query on GOL

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CA [auth B],
DA [auth B],
J [auth A],
K [auth A]
GLYCEROL
C3 H8 O3
PEDCQBHIVMGVHV-UHFFFAOYSA-N
DMS
Query on DMS

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P [auth A]DIMETHYL SULFOXIDE
C2 H6 O S
IAZDPXIOMUYVGZ-UHFFFAOYSA-N
ZN
Query on ZN

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C [auth A],
V [auth B]
ZINC ION
Zn
PTFCDOFLOPIGGS-UHFFFAOYSA-N
NA
Query on NA

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O [auth A]SODIUM ION
Na
FKNQFGJONOIPTF-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.70 Å
  • R-Value Free: 0.181 
  • R-Value Work: 0.154 
  • R-Value Observed: 0.155 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 44.07α = 90
b = 84.87β = 97.81
c = 77.22γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
XDSdata reduction
SCALAdata scaling
PHASERphasing

Structure Validation

View Full Validation Report



Ligand Structure Quality Assessment 


Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
Polish Ministry of Science and Higher EducationPolandMobility Plus Program

Revision History  (Full details and data files)

  • Version 1.0: 2017-03-01
    Type: Initial release
  • Version 1.1: 2017-03-15
    Changes: Database references
  • Version 1.2: 2017-08-16
    Changes: Data collection
  • Version 2.0: 2018-12-19
    Changes: Advisory, Atomic model, Data collection, Derived calculations, Structure summary
  • Version 2.1: 2019-08-21
    Changes: Data collection, Derived calculations
  • Version 3.0: 2023-11-15
    Changes: Atomic model, Data collection, Database references, Derived calculations, Refinement description
  • Version 3.1: 2024-01-10
    Changes: Refinement description