2BEI

X-ray structure of thialysine n-acetyltransferase (SSAT2) from homo sapiens

PDB DOI: https://doi.org/10.2210/pdb2BEI/pdb

Classification: TRANSFERASE
Organism(s): Homo sapiens
Expression System: Escherichia coli
Mutation(s): Yes

Deposited: 2005-10-24 Released: 2005-11-01
Deposition Author(s): Wesenberg, G.E., Phillips Jr., G.N., Han, B.W., Bitto, E., Bingman, C.A., Bae, E., Center for Eukaryotic Structural Genomics (CESG)

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 1.84 Å
R-Value Free: 0.249
R-Value Work: 0.204
R-Value Observed: 0.207

wwPDB Validation 3D Report Full Report

Ligand Structure Quality Assessment

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

Re-refinement Note

A newer entry is available that reflects an alternative modeling of the original data: 2Q4V

Literature

Crystal structure of Homo sapiens thialysine Nepsilon-acetyltransferase (HsSSAT2) in complex with acetyl coenzyme A.

Han, B.W., Bingman, C.A., Wesenberg, G.E., Phillips, G.N.

(2006) Proteins 64: 288-293

PubMed: 16596569 Search on PubMed
DOI: https://doi.org/10.1002/prot.20967
Primary Citation of Related Structures:
2BEI

Organizational Affiliation

Department of Biochemistry, University of Wisconsin-Madison, 53706-1544, USA.

Macromolecule Content

Total Structure Weight: 39.27 kDa
Atom Count: 2,880
Modelled Residue Count: 315
Deposited Residue Count: 340
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
Diamine acetyltransferase 2	A, B	170	Homo sapiens	Mutation(s): 2 Gene Names: SAT2, SSAT2 EC: 2.3.1.57
UniProt & NIH Common Fund Data Resources
Find proteins for Q96F10 (Homo sapiens) Explore Q96F10 Go to UniProtKB: Q96F10
PHAROS: Q96F10 GTEx: ENSG00000141504
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	Q96F10
Sequence Annotations Expand
Reference Sequence

Small Molecules

Ligands 1 Unique
ID	Chains	Name / Formula / InChI Key	2D Diagram	3D Interactions
ACO Query on ACO Download Ideal Coordinates CCD File SDF format, chain C [auth A] MOL2 format, chain C [auth A]	C [auth A]	*ACETYL COENZYME A** C₂₃ H₃₈ N₇ O₁₇ P₃ S ZSLZBFCDCINBPY-ZSJPKINUSA-N		Interactions Focus chain C [auth A] Interactions & Density Focus chain C [auth A]

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

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 1.84 Å
R-Value Free: 0.249
R-Value Work: 0.204
R-Value Observed: 0.207
Space Group: P 2₁ 2₁ 2₁

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 54.583	α = 90
b = 83.621	β = 90
c = 87.548	γ = 90

Software Package:

Software Name	Purpose
DENZO	data reduction
SCALEPACK	data scaling
SHARP	phasing
DM	phasing
REFMAC	refinement
PDB_EXTRACT	data extraction
SOLOMON	phasing
ARP/wARP	model building

Structure Validation

View Full Validation Report

Ligand Structure Quality Assessment

Entry History

Deposition Data

Released Date: 2005-11-01

Deposition Author(s):

Wesenberg, G.E.

Phillips Jr., G.N.

Center for Eukaryotic Structural Genomics (CESG)

Revision History (Full details and data files)

Version 1.0: 2005-11-01
Type: Initial release
Version 1.1: 2008-05-01
Changes: Version format compliance
Version 1.2: 2011-07-13
Changes: Version format compliance
Version 1.3: 2017-10-18
Changes: Refinement description

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.