3F2Z

Crystal structure of the C-terminal domain of a chitobiase (BF3579) from Bacteroides fragilis, Northeast Structural Genomics Consortium Target BfR260B

PDB DOI: https://doi.org/10.2210/pdb3F2Z/pdb

Classification: structural genomics, unknown function
Organism(s): Bacteroides fragilis NCTC 9343
Expression System: Escherichia coli
Mutation(s): No

Deposited: 2008-10-30 Released: 2008-11-18
Deposition Author(s): Forouhar, F., Lew, S., Seetharaman, J., Janjua, H., Xiao, R., Foote, E.L., Ciccosanti, C., Lee, D., Nair, R., Everett, J.K., Acton, T.B., Rost, B., Montelione, G.T., Hunt, J.F., Tong, L., Northeast Structural Genomics Consortium (NESG)

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 1.30 Å
R-Value Free: 0.175
R-Value Work: 0.155
R-Value Observed: 0.156

wwPDB Validation 3D Report Full Report

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

Literature

Crystal structure of the C-terminal domain of a chitobiase (BF3579) from Bacteroides fragilis, Northeast Structural Genomics Consortium Target BfR260B

Forouhar, F., Lew, S., Seetharaman, J., Janjua, H., Xiao, R., Foote, E.L., Ciccosanti, C., Lee, D., Nair, R., Everett, J.K., Acton, T.B., Rost, B., Montelione, G.T., Hunt, J.F., Tong, L.

To be published.

Macromolecule Content

Total Structure Weight: 17.9 kDa
Atom Count: 1,554
Modelled Residue Count: 149
Deposited Residue Count: 159
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
uncharacterized protein BF3579	A	159	Bacteroides fragilis NCTC 9343	Mutation(s): 0 Gene Names: BF3579
UniProt
Find proteins for Q5L9G5 (Bacteroides fragilis (strain ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019 / LMG 10263 / NCTC 9343 / Onslow / VPI 2553 / EN-2)) Explore Q5L9G5 Go to UniProtKB: Q5L9G5
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	Q5L9G5
Sequence Annotations Expand
Reference Sequence

Small Molecules

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

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 1.30 Å
R-Value Free: 0.175
R-Value Work: 0.155
R-Value Observed: 0.156
Space Group: P 2₁ 2₁ 2₁

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 47.893	α = 90
b = 51.684	β = 90
c = 63.96	γ = 90

Software Package:

Software Name	Purpose
ADSC	data collection
SOLVE	phasing
RESOLVE	model building
CNS	refinement
HKL-2000	data reduction
SCALEPACK	data scaling
RESOLVE	phasing

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 2008-11-18

Deposition Author(s):

Northeast Structural Genomics Consortium (NESG)

Revision History (Full details and data files)

Version 1.0: 2008-11-18
Type: Initial release
Version 1.1: 2011-07-13
Changes: Source and taxonomy, Version format compliance
Version 1.2: 2017-10-25
Changes: Refinement description
Version 1.3: 2023-12-27
Changes: Data collection, Database references, Derived calculations
Version 1.4: 2024-10-16
Changes: Structure summary