9PQK: Maltose/maltodextrin-binding periplasmic protein

Crystal structure of maltose binding protein (Apo), mutant Trp10 to 4-Fluorotryptophan. Determined by X-ray diffraction at 1.87 Å resolution. Released 5 Aug 2026.

Method
X-ray diffraction
Resolution
1.87 Å
Organism
Escherichia coli
Chains
1
Atoms
3,028
Mol. weight
41.38 kDa
Ligands
CD
Released
5 Aug 2026

Explore 9PQK in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9PQK contains 24 α-helices and 24 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 24 helices, 24 β-strands

ElementResiduesLengthSheet
α-helix2-32
β-strand6-1051
α-helix17-3115
β-strand34-3851
α-helix43-519
β-strand59-6351
α-helix64-663
α-helix67-726
β-strand7612
α-helix77-793
α-helix83-875
β-strand8913
α-helix91-955
β-strand98-9924
β-strand102-10324
β-strand106-11161
β-strand114-11855
β-strand12816
α-helix129-1313
α-helix132-1409
β-strand145-14735
α-helix154-1618
β-strand167-17267
β-strand175-18287
α-helix186-20015
α-helix210-2189
β-strand222-22765
α-helix229-2346
β-strand242-24545
α-helix246-2483
β-strand24916
β-strand25018
β-strand25318
α-helix254-2552
β-strand258-25929
β-strand260-26671
β-strand26712
α-helix273-2797
α-helix280-2845
α-helix287-29610
β-strand301-30221
β-strand30413
α-helix305-3117
α-helix315-32612
β-strand328-32929
α-helix330-3312
α-helix336-35217
α-helix357-36913

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Maltose/maltodextrin-binding periplasmic proteinAprotein370Escherichia coliP0AEY0 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>9PQK_1 Maltose/maltodextrin-binding periplasmic protein (chains A)
KIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDII
FWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKD
LLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDIKD
VGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKV
NYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLG
AVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQAVDEA
LKDAQTRITK

Ligands and cofactors

IDNameFormulaCopies
CDCadmium ionCd4

Water and common crystallization additives (NA, EDO) are not listed.

Primary citation

Structural accomodations of tryptophan 4-substitutions in maltose binding protein. Habel, E., Huber, T. To be published.

Other PDB entries of the same protein (UniProt P0AEY0 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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