2QJF

Crystal structure of ATP-sulfurylase domain of human PAPS synthetase 1

PDB DOI: https://doi.org/10.2210/pdb2QJF/pdb

Classification: TRANSFERASE
Organism(s): Homo sapiens
Expression System: Escherichia coli
Mutation(s): No

Deposited: 2007-07-07 Released: 2008-11-11
Deposition Author(s): Sekulic, N., Lavie, A.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 2.20 ?
R-Value Free: 0.225
R-Value Work: 0.168
R-Value Observed: 0.173

Starting Model: experimental
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Ligand Structure Quality Assessment

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

Literature

ATP-sulfurylase domain of human bifunctional PAPS-synthetase oscillates between dimeric and monomeric forms

Sekulic, N., Paarmann, I., Konrad, M., Lavie, A.

To be published.

Macromolecule Content

Total Structure Weight: 94.35 kDa
Atom Count: 7,017
Modelled Residue Count: 781
Deposited Residue Count: 810
Unique protein chains: 1

Macromolecules

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(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthetase 1	A, B	405	Homo sapiens	Mutation(s): 0 Gene Names: PAPSS1, ATPSK1, PAPSS EC: 2.7.7.4 (PDB Primary Data), 2.7.1.25 (UniProt)
UniProt & NIH Common Fund Data Resources
Find proteins for O43252 (Homo sapiens) Explore O43252 Go to UniProtKB: O43252
PHAROS: O43252 GTEx: ENSG00000138801
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	O43252
Sequence Annotations Expand
Reference Sequence

Small Molecules

Ligands 2 Unique
ID	Chains	Name / Formula / InChI Key	2D Diagram	3D Interactions
ADX Query on ADX Download Ideal Coordinates CCD File SDF format, chain D [auth A] SDF format, chain F [auth B] MOL2 format, chain D [auth A] MOL2 format, chain F [auth B] mmCIF format, chain D [auth A] mmCIF format, chain F [auth B]	D [auth A], F [auth B]	ADENOSINE-5'-PHOSPHOSULFATE C₁₀ H₁₄ N₅ O₁₀ P S IRLPACMLTUPBCL-KQYNXXCUSA-N		Interactions Focus chain D [auth A] Focus chain F [auth B] Interactions & Density Focus chain D [auth A] Focus chain F [auth B]
K Query on K Download Ideal Coordinates CCD File SDF format, chain C [auth A] SDF format, chain E [auth B] MOL2 format, chain C [auth A] MOL2 format, chain E [auth B] mmCIF format, chain C [auth A] mmCIF format, chain E [auth B]	C [auth A], E [auth B]	POTASSIUM ION K NPYPAHLBTDXSSS-UHFFFAOYSA-N		Interactions Focus chain C [auth A] Focus chain E [auth B] Interactions & Density Focus chain C [auth A] Focus chain E [auth B]

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 2.20 ?
R-Value Free: 0.225
R-Value Work: 0.168
R-Value Observed: 0.173
Space Group: P 1 2₁ 1

Unit Cell:

Length ( ? )	Angle ( ? )
a = 63.1	α = 90
b = 99.9	β = 113
c = 75.9	γ = 90

Software Package:

Software Name	Purpose
REFMAC	refinement
HKL-2000	data collection
XDS	data reduction
XSCALE	data scaling
AMoRE	phasing

Structure Validation

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Ligand Structure Quality Assessment

Entry History

Deposition Data

Released Date: 2008-11-11

Deposition Author(s):

Sekulic, N.

Lavie, A.

Revision History (Full details and data files)

Version 1.0: 2008-11-11
Type: Initial release
Version 1.1: 2011-07-13
Changes: Version format compliance
Version 1.2: 2023-08-30
Changes: Data collection, Database references, Derived calculations, Refinement description

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2QJF

Crystal structure of ATP-sulfurylase domain of human PAPS synthetase 1

ATP-sulfurylase domain of human bifunctional PAPS-synthetase oscillates between dimeric and monomeric forms

Entity ID: 1

UniProt & NIH Common Fund Data Resources

Entity Groups

Sequence Annotations

Expand

Experimental Data

Structure Validation

Ligand Structure Quality Assessment

Deposition Data

Revision History (Full details and data files)