3BU2

Crystal structure of a tRNA-binding protein from Staphylococcus saprophyticus subsp. saprophyticus. Northeast Structural Genomics Consortium target SyR77

PDB DOI: https://doi.org/10.2210/pdb3BU2/pdb

Classification: RNA BINDING PROTEIN
Organism(s): Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 = NCTC 7292
Expression System: Escherichia coli
Mutation(s): No

Deposited: 2007-12-31 Released: 2008-01-22
Deposition Author(s): Seetharaman, J., Su, M., Forouhar, F., Wang, D., Fang, Y., Cunningham, K., Ma, L.-C., Xia, R., Liu, J., Baran, M.C., 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: 2.70 Å
R-Value Free: 0.273
R-Value Work: 0.250
R-Value Observed: 0.250

wwPDB Validation 3D Report Full Report

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

Literature

Crystal structure of a tRNA-binding protein from Staphylococcus saprophyticus subsp. saprophyticus.

Seetharaman, J., Su, M., Forouhar, F., Wang, D., Fang, Y., Cunningham, K., Ma, L.-C., Xia, R., Liu, J., Baran, M.C., Acton, T.B., Rost, B., Montelione, G.T., Hunt, J.F., Tong, L.

To be published.

Macromolecule Content

Total Structure Weight: 86.71 kDa
Atom Count: 6,099
Modelled Residue Count: 780
Deposited Residue Count: 796
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
Putative tRNA-binding protein	A, B, C, D	199	Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 = NCTC 7292	Mutation(s): 0 Gene Names: SSP1021
UniProt
Find proteins for Q49YH3 (Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41)) Explore Q49YH3 Go to UniProtKB: Q49YH3
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	Q49YH3
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: 2.70 Å
R-Value Free: 0.273
R-Value Work: 0.250
R-Value Observed: 0.250
Space Group: P 2₁ 2₁ 2₁

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 75.902	α = 90
b = 79.795	β = 90
c = 139.135	γ = 90

Software Package:

Software Name	Purpose
CNS	refinement
MAR345dtb	data collection
HKL-2000	data reduction
HKL-2000	data scaling
SHELXD	phasing

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 2008-01-22

Deposition Author(s):

Seetharaman, J.

Montelione, G.T.

Northeast Structural Genomics Consortium (NESG)

Revision History (Full details and data files)

Version 1.0: 2008-01-22
Type: Initial release
Version 1.1: 2011-07-13
Changes: Version format compliance
Version 1.2: 2018-01-24
Changes: Database references, Structure summary

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.