3DTO

Crystal structure of the metal-dependent HD domain-containing hydrolase BH2835 from Bacillus halodurans, Northeast Structural Genomics Consortium Target BhR130.

PDB DOI: https://doi.org/10.2210/pdb3DTO/pdb

Classification: structural genomics, unknown function
Organism(s): Halalkalibacterium halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125)
Expression System: Escherichia coli
Mutation(s): No

Deposited: 2008-07-15 Released: 2008-09-09
Deposition Author(s): Forouhar, F., Su, M., Seetharaman, J., Janjua, H., Fang, Y., Xiao, R., Cunningham, K., Ma, L.-C., Owen, L.A., Wang, D., Tong, S., Everett, J.K., Acton, T.B., Montelione, G.T., Tong, L., Hunt, J.F., Northeast Structural Genomics Consortium (NESG)

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 3.30 Å
R-Value Free: 0.292
R-Value Work: 0.248
R-Value Observed: 0.248

wwPDB Validation 3D Report Full Report

This is version 1.1 of the entry. See complete history.

Literature

Crystal structure of the metal-dependent HD domain-containing hydrolase BH2835 from Bacillus halodurans, Northeast Structural Genomics Consortium Target BhR130.

Forouhar, F., Su, M., Seetharaman, J., Janjua, H., Fang, Y., Xiao, R., Cunningham, K., Ma, L.-C., Owen, L.A., Wang, D., Tong, S., Everett, J.K., Acton, T.B., Montelione, G.T., Tong, L., Hunt, J.F.

To be published.

Macromolecule Content

Total Structure Weight: 104.82 kDa
Atom Count: 6,132
Modelled Residue Count: 756
Deposited Residue Count: 892
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
BH2835 protein	A, B, C, D	223	N/A	Mutation(s): 0 Gene Names: BH2835
UniProt
Find proteins for Q9K916 (Halalkalibacterium halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125)) Explore Q9K916 Go to UniProtKB: Q9K916
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	Q9K916
Sequence Annotations Expand
Reference Sequence

Small Molecules

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

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 3.30 Å
R-Value Free: 0.292
R-Value Work: 0.248
R-Value Observed: 0.248
Space Group: P 1 2₁ 1

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 97.564	α = 90
b = 47.987	β = 89.99
c = 111.159	γ = 90

Software Package:

Software Name	Purpose
CNS	refinement
ADSC	data collection
DENZO	data reduction
SCALEPACK	data scaling
SnB	phasing

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 2008-09-09

Deposition Author(s):

Seetharaman, J.

Montelione, G.T.

Northeast Structural Genomics Consortium (NESG)

Revision History (Full details and data files)

Version 1.0: 2008-09-09
Type: Initial release
Version 1.1: 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.