3SEW: Maltose-binding periplasmic protein

Zn-mediated Polymer of Maltose-binding Protein A216H/K220H by Synthetic Symmetrization (Form I). Determined by X-ray diffraction at 1.55 Å resolution. Released 21 Sept 2011.

Method: X-ray diffraction
Resolution: 1.55 Å
Organism: Escherichia coli
Chains: 1
Atoms: 3,237
Mol. weight: 41.71 kDa
Ligands: ZN
Released: 21 Sept 2011

Explore 3SEW in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3SEW contains 25 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: 25 helices, 24 β-strands

Element	Residues	Length	Sheet
β-strand	7-11	5	1
α-helix	18-32	15
β-strand	35-39	5	1
α-helix	44-52	9
β-strand	60-64	5	1
α-helix	65-67	3
α-helix	68-73	6
β-strand	77	1	2
α-helix	78-80	3
α-helix	84-87	4
β-strand	90	1	3
α-helix	92-97	6
β-strand	99-100	2	4
β-strand	103-104	2	4
β-strand	107-112	6	1
β-strand	115-119	5	5
β-strand	129	1	6
α-helix	130-132	3
α-helix	133-141	9
β-strand	146-148	3	5
α-helix	155-157	3
α-helix	159-164	6
β-strand	168-173	6	7
β-strand	176-183	8	7
α-helix	187-201	15
α-helix	211-219	9
β-strand	223-228	6	5
α-helix	230-232	3
α-helix	233-239	7
β-strand	243-246	4	5
α-helix	247-249	3
β-strand	250	1	6
β-strand	251	1	8
β-strand	254	1	8
α-helix	258	1
β-strand	259-260	2	9
β-strand	261-267	7	1
β-strand	268	1	2
α-helix	274-280	7
α-helix	281-285	5
α-helix	288-297	10
β-strand	302-303	2	1
β-strand	305	1	3
α-helix	306-312	7
α-helix	316-327	12
β-strand	329-330	2	9
α-helix	331-332	2
α-helix	337-353	17
α-helix	358-369	12

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Maltose-binding periplasmic protein	A	protein	372	Escherichia coli	P0AEX9 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>3SEW_1 Maltose-binding periplasmic protein (chains A)
MKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDI
IFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNK
DLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDIK
DVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEHAFNHGETAMTINGPWAWSNIDTSK
VNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPL
GAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDA
ALAAAQTNAAAA

Ligands and cofactors

ID	Name	Formula	Copies
ZN	Zinc ion	Zn	1

Water and common crystallization additives (GOL, CL) are not listed.

Primary citation

An approach to crystallizing proteins by metal-mediated synthetic symmetrization. Laganowsky, A., Zhao, M., Soriaga, A.B. et al. Protein Sci (2011) 20:1876-1890. DOI 10.1002/pro.727 · 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
9CLC 1.48 Å, Crystal structure of maltose binding protein (Apo), mutant Trp10 to 4-Cyanotryptophan

Browse structure collections

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