9CLC: Maltose/maltodextrin-binding periplasmic protein

Crystal structure of maltose binding protein (Apo), mutant Trp10 to 4-Cyanotryptophan. Determined by X-ray diffraction at 1.48 Å resolution. Released 18 Dec 2024.

Method: X-ray diffraction
Resolution: 1.48 Å
Organism: Escherichia coli
Chains: 1
Atoms: 3,333
Mol. weight: 42.81 kDa
Ligands: CD
Released: 18 Dec 2024

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

Secondary structure: helices and β-sheets

9CLC contains 23 α-helices and 23 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: 23 helices, 23 β-strands

Element	Residues	Length	Sheet
α-helix	2-3	2
β-strand	6-10	5	1
α-helix	17-31	15
β-strand	34-38	5	1
α-helix	43-51	9
β-strand	59-63	5	1
α-helix	64-72	9
β-strand	76	1	2
α-helix	77-79	3
α-helix	83-86	4
β-strand	89	1	3
α-helix	91-96	6
β-strand	98-99	2	4
β-strand	102-103	2	4
β-strand	106-111	6	1
β-strand	114-118	5	5
β-strand	128	1	6
α-helix	129-131	3
α-helix	132-141	10
β-strand	145-147	3	5
α-helix	154-163	10
β-strand	167-172	6	7
β-strand	175-182	8	7
α-helix	186-200	15
α-helix	210-218	9
β-strand	222-227	6	5
α-helix	229-234	6
β-strand	242-245	4	5
α-helix	246-248	3
β-strand	249-250	2	6
β-strand	253-254	2	6
α-helix	255	1
β-strand	258-259	2	8
β-strand	260-266	7	1
β-strand	267	1	2
α-helix	273-279	7
α-helix	280-284	5
α-helix	287-296	10
β-strand	301-302	2	1
β-strand	304	1	3
α-helix	305-311	7
α-helix	315-326	12
β-strand	328-329	2	8
α-helix	330-331	2
α-helix	336-352	17
α-helix	357-369	13

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Maltose/maltodextrin-binding periplasmic protein	A	protein	373	Escherichia coli	P0AEX9 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>9CLC_1 Maltose/maltodextrin-binding periplasmic protein (chains A)
GHMKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGP
DIIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIY
NKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYD
IKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDT
SKVNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDK
PLGAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQAV
DEALKDAQTRITK

Ligands and cofactors

ID	Name	Formula	Copies
CD	Cadmium ion	Cd	3

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

Primary citation

Rendering Proteins Fluorescent Inconspicuously: Genetically Encoded 4-Cyanotryptophan Conserves Their Structure and Enables the Detection of Ligand Binding Sites. Qianzhu, H., Abdelkader, E.H., Welegedara, A.P. et al. Angew Chem Int Ed Engl (2025) 64:e202421000-e202421000. DOI 10.1002/anie.202421000 · PubMed

Other PDB entries of the same protein (UniProt P0AEX9 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8C8F 1.15 Å, Crystal structure of the E. coli maltodextrin-binding protein
4EXK 1.28 Å, A chimera protein containing MBP fused to the C-terminal domain of the uncharacterized…
3Q27 1.3 Å, Cyrstal structure of human alpha-synuclein (32-57) fused to maltose binding protein (MBP)
7KD4 1.31 Å, Structure of the C-terminal domain of the Menangle virus phosphoprotein (residues 329…
5M13 1.37 Å, Synthetic nanobody in complex with MBP
5HZ7 1.43 Å, High-resolution crystal structure of the minor DNA-binding pilin ComP from Neisseria…
5H7Q 1.45 Å, Crystal structure of human MNDA PYD domain with MBP tag
6XDS 1.47 Å, Crystal structure of MBP-TREM2 Ig domain fusion with fragment,…
4IRL 1.47 Å, X-ray structure of the CARD domain of zebrafish GBP-NLRP1 like protein
8SVY 1.47 Å, MBP-Mcl1 in complex with ligand 10
3MP6 1.48 Å, Complex Structure of Sgf29 and dimethylated H3K4
3O3U 1.5 Å, Crystal Structure of Human Receptor for Advanced Glycation Endproducts (RAGE)

Browse structure collections

About this viewer

MolViewer shows 9CLC directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.