5K27

Crystal structure of ancestral protein ancMT of ADP-dependent sugar kinases family.

PDB DOI: https://doi.org/10.2210/pdb5K27/pdb

Classification: TRANSFERASE
Organism(s): synthetic construct
Expression System: Escherichia coli
Mutation(s): No

Deposited: 2016-05-18 Released: 2017-05-24
Deposition Author(s): Castro-Fernandez, V., Herrera-Morande, A., Zamora, R., Merino, F., Pereira, H.M., Brandao-Neto, J., Garratt, R., Guixe, V.
Funding Organization(s): FONDECYT

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 2.58 Å
R-Value Free: 0.258
R-Value Work: 0.214
R-Value Observed: 0.216

wwPDB Validation 3D Report Full Report

Ligand Structure Quality Assessment

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

Literature

Reconstructed ancestral enzymes reveal that negative selection drove the evolution of substrate specificity in ADP-dependent kinases.

Castro-Fernandez, V., Herrera-Morande, A., Zamora, R., Merino, F., Gonzalez-Ordenes, F., Padilla-Salinas, F., Pereira, H.M., Brandao-Neto, J., Garratt, R.C., Guixe, V.

(2017) J Biol Chem 292: 21218-21218

PubMed: 29273585 Search on PubMedSearch on PubMed Central
DOI: https://doi.org/10.1074/jbc.AAC117.001147
Primary Citation of Related Structures:
5K27, 5KKG

Macromolecule Content

Total Structure Weight: 109.96 kDa
Atom Count: 6,889
Modelled Residue Count: 902
Deposited Residue Count: 944
Unique protein chains: 1

Macromolecules

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(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
ancMT	A, B	472	synthetic construct	Mutation(s): 0 EC: 2.7.1.146 (PDB Primary Data), 2.7.1.147 (PDB Primary Data)
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
Sequence Annotations Expand
Reference Sequence

Small Molecules

Ligands 2 Unique
ID	Chains	Name / Formula / InChI Key	2D Diagram	3D Interactions
AMP Query on AMP Download Ideal Coordinates CCD File SDF format, chain C [auth A] SDF format, chain H [auth B] MOL2 format, chain C [auth A] MOL2 format, chain H [auth B]	C [auth A], H [auth B]	ADENOSINE MONOPHOSPHATE C₁₀ H₁₄ N₅ O₇ P UDMBCSSLTHHNCD-KQYNXXCUSA-N		Interactions Focus chain C [auth A] Focus chain H [auth B] Interactions & Density Focus chain C [auth A] Focus chain H [auth B]
IOD Query on IOD Download Ideal Coordinates CCD File SDF format, chain D [auth A] SDF format, chain E [auth A] SDF format, chain F [auth A] SDF format, chain G [auth A] SDF format, chain I [auth B] MOL2 format, chain D [auth A] MOL2 format, chain E [auth A] MOL2 format, chain F [auth A] MOL2 format, chain G [auth A] MOL2 format, chain I [auth B]	D [auth A], E [auth A], F [auth A], G [auth A], I [auth B]	IODIDE ION I XMBWDFGMSWQBCA-UHFFFAOYSA-M		Interactions Focus chain D [auth A] Focus chain E [auth A] Focus chain F [auth A] Focus chain G [auth A] Focus chain I [auth B] Interactions & Density Focus chain D [auth A] Focus chain E [auth A] Focus chain F [auth A] Focus chain G [auth A] Focus chain I [auth B]

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 2.58 Å
R-Value Free: 0.258
R-Value Work: 0.214
R-Value Observed: 0.216
Space Group: P 4₁ 2₁ 2

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 132.354	α = 90
b = 132.354	β = 90
c = 116.773	γ = 90

Software Package:

Software Name	Purpose
Aimless	data scaling
PHENIX	refinement
PDB_EXTRACT	data extraction
XDS	data reduction
PHASER	phasing

Structure Validation

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Ligand Structure Quality Assessment

Entry History & Funding Information

Deposition Data

Released Date: 2017-05-24

Deposition Author(s):

Funding Organization	Location	Grant Number
FONDECYT	Chile	1150460

Revision History (Full details and data files)

Version 1.0: 2017-05-24
Type: Initial release
Version 1.1: 2018-07-04
Changes: Data collection, Database references
Version 1.2: 2023-09-27
Changes: Data collection, Database references, Refinement description

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5K27

Crystal structure of ancestral protein ancMT of ADP-dependent sugar kinases family.

Reconstructed ancestral enzymes reveal that negative selection drove the evolution of substrate specificity in ADP-dependent kinases.

Entity ID: 1

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)