1V9I

Crystal Structure Analysis of the site specific mutant (Q253C) of bovine carbonic anhydrase II

PDB DOI: https://doi.org/10.2210/pdb1V9I/pdb

Classification: LYASE
Organism(s): Bos taurus
Expression System: Escherichia coli
Mutation(s): Yes

Deposited: 2004-01-26 Released: 2004-02-10
Deposition Author(s): Saito, R., Sato, T., Ikai, A., Tanaka, N.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 2.95 Å
R-Value Free: 0.346
R-Value Work: 0.247

wwPDB Validation 3D Report Full Report

This is version 1.4 of the entry. See complete history.

Literature

Crystal Structure Analysis of the site specific mutant (Q253C) of bovine carbonic anhydrase II

Saito, R., Sato, T., Ikai, A., Tanaka, N.

To be published.

Macromolecule Content

Total Structure Weight: 29.32 kDa
Atom Count: 2,069
Modelled Residue Count: 261
Deposited Residue Count: 261
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 II	A [auth C]	261	Bos taurus	Mutation(s): 1 EC: 4.2.1.1
UniProt
Find proteins for P00921 (Bos taurus) Explore P00921 Go to UniProtKB: P00921
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	P00921
Sequence Annotations Expand
Reference Sequence

Small Molecules

Ligands 1 Unique
ID	Chains	Name / Formula / InChI Key	2D Diagram	3D Interactions
ZN Query on ZN Download Ideal Coordinates CCD File SDF format, chain B [auth C] MOL2 format, chain B [auth C]	B [auth C]	ZINC ION Zn PTFCDOFLOPIGGS-UHFFFAOYSA-N		Interactions Focus chain B [auth C] Interactions & Density Focus chain B [auth C]

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 2.95 Å
R-Value Free: 0.346
R-Value Work: 0.247
Space Group: P 3₁ 2 1

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 73.1	α = 90
b = 73.1	β = 90
c = 116	γ = 120

Software Package:

Software Name	Purpose
CNS	refinement
MOSFLM	data reduction
CCP4	data scaling
EPMR	phasing

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 2004-02-10

Deposition Author(s):

Revision History (Full details and data files)

Version 1.0: 2004-02-10
Type: Initial release
Version 1.1: 2008-04-27
Changes: Version format compliance
Version 1.2: 2011-07-13
Changes: Version format compliance
Version 1.3: 2021-11-10
Changes: Database references, Derived calculations
Version 1.4: 2023-12-27
Changes: Data collection

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.