2FVZ

Human Inositol Monophosphosphatase 2

PDB DOI: https://doi.org/10.2210/pdb2FVZ/pdb

Classification: HYDROLASE
Organism(s): Homo sapiens
Expression System: Escherichia coli BL21(DE3)
Mutation(s): No

Deposited: 2006-01-31 Released: 2006-02-21
Deposition Author(s): Ogg, D., Hallberg, B.M., Arrowsmith, C., Berglund, H., Collins, R., Edwards, A., Ehn, M., Flodin, S., Graslund, S., Hammarstrom, M., Hogbom, M., Holmberg-Schiavone, L., Kotenyova, T., Kursula, P., Nilsson-Ehle, P., Nordlund, P., Nyman, T., Persson, C., Sagemark, J., Stenmark, P., Sundstrom, M., Van Den Berg, S., Weigelt, J., Thorsell, A.G., Structural Genomics Consortium (SGC)

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 2.40 Å
R-Value Free: 0.297
R-Value Work: 0.211
R-Value Observed: 0.214

wwPDB Validation 3D Report Full Report

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

Literature

Structure of Human Inositol Monophosphatase 2

Thorsell, A.G., Ogg, D., Berglund, H., Collins, R., Ehn, M., Flodin, S., Graslund, S., Hammarstrom, M., Hogbom, M., Holmberg-Schiavone, L., Kotenyova, T., Kursula, P., Nilsson-Ehle, P., Persson, C., Nordlund, P., Nyman, T., Sagemark, J., Stenmark, P., Van Den Berg, S., Weigelt, J., Hallberg, B.M.

To be published.

Macromolecule Content

Total Structure Weight: 119.74 kDa
Atom Count: 7,516
Modelled Residue Count: 976
Deposited Residue Count: 1,092
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
Inositol monophosphatase 2	A, B, C, D	273	Homo sapiens	Mutation(s): 0 Gene Names: IMPA2, IMP.18P EC: 3.1.3.25
UniProt & NIH Common Fund Data Resources
Find proteins for O14732 (Homo sapiens) Explore O14732 Go to UniProtKB: O14732
PHAROS: O14732 GTEx: ENSG00000141401
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	O14732
Sequence Annotations Expand
Reference Sequence

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 2.40 Å
R-Value Free: 0.297
R-Value Work: 0.211
R-Value Observed: 0.214
Space Group: P 1 2₁ 1

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 65.03	α = 90
b = 96.95	β = 90.03
c = 106.97	γ = 90

Software Package:

Software Name	Purpose
SHELX	refinement
PDB_EXTRACT	data extraction
XDS	data reduction
XSCALE	data scaling
MOLREP	phasing
SHELXL-97	refinement

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 2006-02-21

Deposition Author(s):

Hammarstrom, M.

Holmberg-Schiavone, L.

Nilsson-Ehle, P.

Van Den Berg, S.

Structural Genomics Consortium (SGC)

Revision History (Full details and data files)

Version 1.0: 2006-02-21
Type: Initial release
Version 1.1: 2008-05-01
Changes: Version format compliance
Version 1.2: 2011-07-13
Changes: Version format compliance
Version 1.3: 2018-05-23
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.