3G9Q | pdb_00003g9q

Crystal structure of the FhuD fold-family BSU3320, a periplasmic binding protein component of a Fep/Fec-like ferrichrome ABC transporter from Bacillus subtilis. Northeast Structural Genomics Consortium Target SR577A

PDB DOI: https://doi.org/10.2210/pdb3G9Q/pdb

Classification: TRANSPORT PROTEIN
Organism(s): Bacillus subtilis subsp. subtilis str. 168
Expression System: Escherichia coli
Mutation(s): No

Deposited: 2009-02-13 Released: 2009-03-03
Deposition Author(s): Forouhar, F., Neely, H., Seetharaman, J., Janjua, H., Mao, L., Xiao, R., Ciccosanti, C., Foote, E.L., Lee, D., Nair, R., Acton, T.B., Rost, B., Montelione, G.T., Tong, L., Hunt, J.F., Northeast Structural Genomics Consortium (NESG)

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 2.60 Å
R-Value Free:
0.291 (Depositor), 0.298 (DCC)
R-Value Work:
0.222 (Depositor), 0.233 (DCC)
R-Value Observed:
0.222 (Depositor)

wwPDB Validation 3D Report Full Report

This is version 1.3 of the entry. See complete history.

Literature

Crystal structure of the FhuD fold-family BSU3320, a periplasmic binding protein component of a Fep/Fec-like ferrichrome ABC transporter from Bacillus subtilis. Northeast Structural Genomics Consortium Target SR577A.

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

To be published.

Macromolecule Content

Total Structure Weight: 31.24 kDa
Atom Count: 2,053
Modelled Residue Count: 258
Deposited Residue Count: 279
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
Ferrichrome-binding protein	A	279	Bacillus subtilis subsp. subtilis str. 168	Mutation(s): 0 Gene Names: BSU33320, fhuD
UniProt
Find proteins for P37580 (Bacillus subtilis (strain 168)) Explore P37580 Go to UniProtKB: P37580
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	P37580
Sequence Annotations Expand
Reference Sequence LOADING

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: 2.60 Å
R-Value Free: 0.291 (Depositor), 0.298 (DCC)
R-Value Work: 0.222 (Depositor), 0.233 (DCC)
R-Value Observed: 0.222 (Depositor)

Space Group: P 2₁ 2₁ 2₁

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 35.517	α = 90
b = 69.898	β = 90
c = 114.169	γ = 90

Software Package:

Software Name	Purpose
ADSC	data collection
SnB	phasing
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: 2009-03-03

Deposition Author(s):

Northeast Structural Genomics Consortium (NESG)

Revision History (Full details and data files)

Version 1.0: 2009-03-03
Type: Initial release
Version 1.1: 2011-07-13
Changes: Source and taxonomy, Version format compliance
Version 1.2: 2017-11-01
Changes: Refinement description
Version 1.3: 2024-11-27
Changes: Data collection, Database references, Derived calculations, Structure summary