1ZXO

X-ray Crystal Structure of Protein Q8A1P1 from Bacteroides thetaiotaomicron. Northeast Structural Genomics Consortium Target BtR25.

PDB DOI: https://doi.org/10.2210/pdb1ZXO/pdb

Classification: UNKNOWN FUNCTION
Organism(s): Bacteroides thetaiotaomicron
Expression System: Escherichia coli
Mutation(s): Yes

Deposited: 2005-06-08 Released: 2005-07-05
Deposition Author(s): Kuzin, A.P., Yong, W., Forouhar, F., Vorobiev, S., Xiao, R., Ma, C., Acton, T., Montelione, G.T., Hunt, J., Tong, L., Northeast Structural Genomics Consortium (NESG)

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 3.20 Å
R-Value Free: 0.297
R-Value Work: 0.241
R-Value Observed: 0.241

wwPDB Validation 3D Report Full Report

This is version 1.2 of the entry. See complete history.

Literature

X-Ray structure of the hypothetical protein Q8A1P1 at the resolution 3.2A. Northeast Structural Genomics Consortium target BtR25.

Kuzin, A.P., Yong, W., Forouhar, F., Vorobiev, S., Xiao, R., Ma, C., Acton, T., Montelione, G.T., Hunt, J., Tong, L.

To be published.

Macromolecule Content

Total Structure Weight: 194.96 kDa
Atom Count: 13,033
Modelled Residue Count: 1,659
Deposited Residue Count: 1,746
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
conserved hypothetical protein Q8A1P1	A B [auth F] C [auth B] D E [auth C] A, B [auth F], C [auth B], D, E [auth C], F [auth E]	291	Bacteroides thetaiotaomicron	Mutation(s): 5
UniProt
Find proteins for Q8A1P1 (Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / VPI-5482 / E50)) Explore Q8A1P1 Go to UniProtKB: Q8A1P1
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	Q8A1P1
Sequence Annotations Expand
Reference Sequence

Small Molecules

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

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 3.20 Å
R-Value Free: 0.297
R-Value Work: 0.241
R-Value Observed: 0.241
Space Group: H 3

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 158.154	α = 90
b = 158.154	β = 90
c = 275.531	γ = 120

Software Package:

Software Name	Purpose
CNS	refinement
DENZO	data reduction
SCALEPACK	data scaling
SOLVE	phasing

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 2005-07-05

Deposition Author(s):

Montelione, G.T.

Northeast Structural Genomics Consortium (NESG)

Revision History (Full details and data files)

Version 1.0: 2005-07-05
Type: Initial release
Version 1.1: 2008-04-30
Changes: Version format compliance
Version 1.2: 2011-07-13
Changes: Version format compliance

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.