2R6G

The Crystal Structure of the E. coli Maltose Transporter

PDB DOI: https://doi.org/10.2210/pdb2R6G/pdb

Classification: HYDROLASE/TRANSPORT PROTEIN
Organism(s): Escherichia coli K-12
Expression System: Escherichia coli
Mutation(s): Yes
Membrane Protein: Yes PDBTMMemProtMD

Deposited: 2007-09-05 Released: 2007-11-27
Deposition Author(s): Oldham, M.L., Khare, D., Quiocho, F.A., Davidson, A.L., Chen, J.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 2.80 Å
R-Value Free: 0.271
R-Value Work: 0.242
R-Value Observed: 0.242

wwPDB Validation 3D Report Full Report

Ligand Structure Quality Assessment

This is version 2.2 of the entry. See complete history.

Macromolecule Content

Total Structure Weight: 215.78 kDa
Atom Count: 14,713
Modelled Residue Count: 1,887
Deposited Residue Count: 1,942
Unique protein chains: 4

Macromolecules

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(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
Maltose/maltodextrin import ATP-binding protein malK	A, B	381	Escherichia coli K-12	Mutation(s): 1 Gene Names: malK EC: 3.6.3.19 Membrane Entity: Yes
UniProt
Find proteins for P68187 (Escherichia coli (strain K12)) Explore P68187 Go to UniProtKB: P68187
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	P68187
Sequence Annotations Expand
Reference Sequence

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Entity ID: 2
Molecule	Chains	Sequence Length	Organism	Details	Image
Maltose-binding periplasmic protein	C [auth E]	370	Escherichia coli K-12	Mutation(s): 0 Gene Names: malE Membrane Entity: Yes
UniProt
Find proteins for P0AEX9 (Escherichia coli (strain K12)) Explore P0AEX9 Go to UniProtKB: P0AEX9
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	P0AEX9
Sequence Annotations Expand
Reference Sequence

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(by identity cutoff) | 3D Structure

Entity ID: 3
Molecule	Chains	Sequence Length	Organism	Details	Image
Maltose transport system permease protein malF	D [auth F]	514	Escherichia coli K-12	Mutation(s): 0 Gene Names: malF Membrane Entity: Yes
UniProt
Find proteins for P02916 (Escherichia coli (strain K12)) Explore P02916 Go to UniProtKB: P02916
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	P02916
Sequence Annotations Expand
Reference Sequence

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(by identity cutoff) | 3D Structure

Entity ID: 4
Molecule	Chains	Sequence Length	Organism	Details	Image
Maltose transport system permease protein malG	E [auth G]	296	Escherichia coli K-12	Mutation(s): 0 Gene Names: malG Membrane Entity: Yes
UniProt
Find proteins for P68183 (Escherichia coli (strain K12)) Explore P68183 Go to UniProtKB: P68183
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	P68183
Sequence Annotations Expand
Reference Sequence

Oligosaccharides

Help

Entity ID: 5
Molecule	Chains	Length	2D Diagram	Glycosylation	3D Interactions
alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose	F [auth C]	2		N/A	Interactions Focus chain F [auth C] Interactions & Density Focus chain F [auth C]
Glycosylation Resources
GlyTouCan: G07411ON GlyCosmos: G07411ON

Small Molecules

Ligands 1 Unique
ID	Chains	Name / Formula / InChI Key	2D Diagram	3D Interactions
ATP Query on ATP Download Ideal Coordinates CCD File SDF format, chain G [auth A] SDF format, chain H [auth B] MOL2 format, chain G [auth A] MOL2 format, chain H [auth B]	G [auth A], H [auth B]	ADENOSINE-5'-TRIPHOSPHATE C₁₀ H₁₆ N₅ O₁₃ P₃ ZKHQWZAMYRWXGA-KQYNXXCUSA-N		Interactions Focus chain G [auth A] Focus chain H [auth B] Interactions & Density Focus chain G [auth A] Focus chain H [auth B]

Biologically Interesting Molecules (External Reference) 1 Unique

Entity ID: 5
ID	Chains	Name	Type/Class	2D Diagram	3D Interactions
PRD_900001 Query on PRD_900001	F [auth C]	alpha-maltose	Oligosaccharide / Nutrient		Interactions Focus chain F [auth C] Interactions & Density Focus chain F [auth C]

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 2.80 Å
R-Value Free: 0.271
R-Value Work: 0.242
R-Value Observed: 0.242
Space Group: P 1

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 73.26	α = 87.13
b = 95.86	β = 82.43
c = 109.99	γ = 75.75

Software Package:

Software Name	Purpose
DENZO	data reduction
SCALEPACK	data scaling
PHASER	phasing
DM	phasing
REFMAC	refinement
PDB_EXTRACT	data extraction
Blu-Ice	data collection
HKL-2000	data reduction
HKL-2000	data scaling

Structure Validation

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Ligand Structure Quality Assessment

Entry History

Deposition Data

Released Date: 2007-11-27

Deposition Author(s):

Revision History (Full details and data files)

Version 1.0: 2007-11-27
Type: Initial release
Version 1.1: 2011-07-13
Changes: Source and taxonomy, Version format compliance
Version 1.2: 2017-10-25
Changes: Refinement description
Version 1.3: 2018-01-24
Changes: Structure summary
Version 2.0: 2020-07-29
Type: Remediation
Reason: Carbohydrate remediation
Changes: Atomic model, Data collection, Database references, Derived calculations, Non-polymer description, Structure summary
Version 2.1: 2021-10-20
Changes: Database references, Structure summary
Version 2.2: 2023-08-30
Changes: Data collection, Refinement description