2I5T

Crystal Structure of hypothetical protein LOC79017 from Homo sapiens

PDB DOI: https://doi.org/10.2210/pdb2I5T/pdb

Classification: STRUCTURAL GENOMICS, UNKNOWN FUNCTION
Organism(s): Homo sapiens
Expression System: Escherichia coli
Mutation(s): Yes

Deposited: 2006-08-25 Released: 2006-09-12
Deposition Author(s): Bae, E., Wesenberg, G.E., Phillips Jr., G.N., Bitto, E., Bingman, C.A., Center for Eukaryotic Structural Genomics (CESG)

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 2.01 Å
R-Value Free: 0.234
R-Value Work: 0.183
R-Value Observed: 0.186

wwPDB Validation 3D Report Full Report

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

Re-refinement Note

A newer entry is available that reflects an alternative modeling of the original data: 2Q53

Literature

Crystal structure of Homo sapiens protein LOC79017.

Bae, E., Bingman, C.A., Aceti, D.J., Phillips Jr., G.N.

(2008) Proteins 70: 588-591

PubMed: 17932939 Search on PubMed
DOI: https://doi.org/10.1002/prot.21719
Primary Citation of Related Structures:
2I5T, 2Q53

Organizational Affiliation

Center for Eukaryotic Structural Genomics, University of Wisconsin-Madison, Madison, Wisconsin 53706, USA.

Macromolecule Content

Total Structure Weight: 42.35 kDa
Atom Count: 2,880
Modelled Residue Count: 338
Deposited Residue Count: 376
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
Protein C7orf24	A, B	188	Homo sapiens	Mutation(s): 4 Gene Names: C7orf24
UniProt & NIH Common Fund Data Resources
Find proteins for O75223 (Homo sapiens) Explore O75223 Go to UniProtKB: O75223
PHAROS: O75223 GTEx: ENSG00000006625
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	O75223
Sequence Annotations Expand
Reference Sequence

Small Molecules

Modified Residues 1 Unique
ID	Chains	Type	Formula	2D Diagram	Parent
MSE Query on MSE	A, B	L-PEPTIDE LINKING	C₅ H₁₁ N O₂ Se		MET

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 2.01 Å
R-Value Free: 0.234
R-Value Work: 0.183
R-Value Observed: 0.186
Space Group: P 2₁ 2₁ 2₁

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 35.052	α = 90
b = 100.138	β = 90
c = 102.498	γ = 90

Software Package:

Software Name	Purpose
DENZO	data reduction
SCALEPACK	data scaling
SHARP	phasing
DM	phasing
REFMAC	refinement
PDB_EXTRACT	data extraction
HKL-2000	data reduction

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 2006-09-12

Deposition Author(s):

Wesenberg, G.E.

Phillips Jr., G.N.

Center for Eukaryotic Structural Genomics (CESG)

Revision History (Full details and data files)

Version 1.0: 2006-09-12
Type: Initial release
Version 1.1: 2008-01-15
Changes: Version format compliance
Version 1.2: 2011-07-13
Changes: Version format compliance
Version 1.3: 2011-08-24
Changes: Structure summary
Version 1.4: 2017-10-18
Changes: Refinement description

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.