3L8N

Crystal Structure of a domain of Brefeldin A-inhibited guanine nucleotide-exchange protein 2 (BrefeldinA-inhibited GEP 2) from Homo sapiens (Human). Northeast Structural Genomics Consortium target id HR5562A

PDB DOI: https://doi.org/10.2210/pdb3L8N/pdb

Classification: Nucleotide-binding protein, Metal-binding protein
Organism(s): Homo sapiens
Expression System: Escherichia coli
Mutation(s): No

Deposited: 2009-12-31 Released: 2010-04-07
Deposition Author(s): Seetharaman, J., Su, M., Forouhar, F., Wang, D., Janjua, H., Cunningham, K., Owens, L., Xiao, R., Liu, J., Baran, M.C., Acton, T.B., Montelione, G.T., Hunt, J.F., Tong, L., Northeast Structural Genomics Consortium (NESG)

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 2.86 Å
R-Value Free: 0.290
R-Value Work: 0.236
R-Value Observed: 0.236

wwPDB Validation 3D Report Full Report

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

Literature

Crystal Structure of a domain of Brefeldin A-inhibited guanine nucleotide-exchange protein 2 (BrefeldinA-inhibited GEP 2) from Homo sapiens (Human). Northeast Structural Genomics Consortium target id HR5562A

Seetharaman, J., Su, M., Forouhar, F., Wang, D., Janjua, H., Cunningham, K., Owens, L., Xiao, R., Liu, J., Baran, M.C., Acton, T.B., Montelione, G.T., Hunt, J.F., Tong, L.

To be published.

Macromolecule Content

Total Structure Weight: 23.79 kDa
Atom Count: 1,300
Modelled Residue Count: 179
Deposited Residue Count: 202
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
Brefeldin A-inhibited guanine nucleotide-exchange protein 2	A	202	Homo sapiens	Mutation(s): 0 Gene Names: ARFGEF2, ARFGEP2, BIG2
UniProt & NIH Common Fund Data Resources
Find proteins for Q9Y6D5 (Homo sapiens) Explore Q9Y6D5 Go to UniProtKB: Q9Y6D5
PHAROS: Q9Y6D5 GTEx: ENSG00000124198
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	Q9Y6D5
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: 2.86 Å
R-Value Free: 0.290
R-Value Work: 0.236
R-Value Observed: 0.236
Space Group: P 3₂

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 53.929	α = 90
b = 53.929	β = 90
c = 75.711	γ = 120

Software Package:

Software Name	Purpose
ADSC	data collection
SHELXS	phasing
CNS	refinement
HKL-2000	data reduction
HKL-2000	data scaling

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 2010-04-07

Deposition Author(s):

Seetharaman, J.

Montelione, G.T.

Northeast Structural Genomics Consortium (NESG)

Revision History (Full details and data files)

Version 1.0: 2010-04-07
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.