1AQ2

PHOSPHOENOLPYRUVATE CARBOXYKINASE

PDB DOI: https://doi.org/10.2210/pdb1AQ2/pdb

Classification: KINASE
Organism(s): Escherichia coli K-12
Expression System: Escherichia coli
Mutation(s): No

Deposited: 1997-08-05 Released: 1998-10-14
Deposition Author(s): Tari, L.W., Matte, A., Goldie, H., Delbaere, L.T.J.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 1.90 Å
R-Value Free: 0.260
R-Value Work: 0.218
R-Value Observed: 0.218

wwPDB Validation 3D Report Full Report

Ligand Structure Quality Assessment

This is version 2.0 of the entry. See complete history.

Literature

Mg(2+)-Mn2+ clusters in enzyme-catalyzed phosphoryl-transfer reactions.

Tari, L.W., Matte, A., Goldie, H., Delbaere, L.T.

(1997) Nat Struct Biol 4: 990-994

PubMed: 9406547 Search on PubMed
DOI: https://doi.org/10.1038/nsb1297-990
Primary Citation of Related Structures:
1AQ2

Macromolecule Content

Total Structure Weight: 60.38 kDa
Atom Count: 4,385
Modelled Residue Count: 534
Deposited Residue Count: 540
Unique protein chains: 1

Macromolecules

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(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
PHOSPHOENOLPYRUVATE CARBOXYKINASE	A	540	Escherichia coli K-12	Mutation(s): 0 EC: 4.1.1.49
UniProt
Find proteins for P22259 (Escherichia coli (strain K12)) Explore P22259 Go to UniProtKB: P22259
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	P22259
Sequence Annotations Expand
Reference Sequence

Small Molecules

Ligands 4 Unique
ID	Chains	Name / Formula / InChI Key	2D Diagram	3D Interactions
ATP Query on ATP Download Ideal Coordinates CCD File SDF format, chain D [auth A] MOL2 format, chain D [auth A]	D [auth A]	ADENOSINE-5'-TRIPHOSPHATE C₁₀ H₁₆ N₅ O₁₃ P₃ ZKHQWZAMYRWXGA-KQYNXXCUSA-N		Interactions Focus chain D [auth A] Interactions & Density Focus chain D [auth A]
PYR Query on PYR Download Ideal Coordinates CCD File SDF format, chain E [auth A] MOL2 format, chain E [auth A]	E [auth A]	PYRUVIC ACID C₃ H₄ O₃ LCTONWCANYUPML-UHFFFAOYSA-N		Interactions Focus chain E [auth A] Interactions & Density Focus chain E [auth A]
MN Query on MN Download Ideal Coordinates CCD File SDF format, chain B [auth A] MOL2 format, chain B [auth A]	B [auth A]	MANGANESE (II) ION Mn WAEMQWOKJMHJLA-UHFFFAOYSA-N		Interactions Focus chain B [auth A] Interactions & Density Focus chain B [auth A]
MG Query on MG Download Ideal Coordinates CCD File SDF format, chain C [auth A] MOL2 format, chain C [auth A]	C [auth A]	MAGNESIUM ION Mg JLVVSXFLKOJNIY-UHFFFAOYSA-N		Interactions Focus chain C [auth A] Interactions & Density Focus chain C [auth A]

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 1.90 Å
R-Value Free: 0.260
R-Value Work: 0.218
R-Value Observed: 0.218
Space Group: C 1 2 1

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 126.19	α = 90
b = 96.61	β = 95.8
c = 46.86	γ = 90

Software Package:

Software Name	Purpose
X-PLOR	model building
X-PLOR	refinement
MADNES	data reduction
CCP4	data scaling
X-PLOR	phasing

Structure Validation

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Ligand Structure Quality Assessment

Entry History

Deposition Data

Released Date: 1998-10-14

Deposition Author(s):

Revision History (Full details and data files)

Version 1.0: 1998-10-14
Type: Initial release
Version 1.1: 2008-03-24
Changes: Version format compliance
Version 1.2: 2011-07-13
Changes: Source and taxonomy, Version format compliance
Version 1.3: 2017-11-29
Changes: Derived calculations, Other
Version 1.4: 2018-04-18
Changes: Data collection
Version 1.5: 2023-08-02
Changes: Database references, Derived calculations, Refinement description
Version 2.0: 2023-11-15
Changes: Atomic model, Data collection

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Help and Resources

1AQ2

PHOSPHOENOLPYRUVATE CARBOXYKINASE

Mg(2+)-Mn2+ clusters in enzyme-catalyzed phosphoryl-transfer reactions.

Entity ID: 1

UniProt

Entity Groups

Sequence Annotations

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Experimental Data

Structure Validation

Ligand Structure Quality Assessment

Deposition Data

Revision History (Full details and data files)