2R6G: E. coli Maltose Transporter

The Crystal Structure of the E. coli Maltose Transporter. Determined by X-ray diffraction at 2.8 Å resolution. Released 27 Nov 2007.

Method: X-ray diffraction
Resolution: 2.8 Å
Organism: Escherichia coli
Chains: 5
Atoms: 14,713
Mol. weight: 215.78 kDa
Ligands: ATP
Released: 27 Nov 2007

Explore 2R6G in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2R6G contains 99 α-helices and 101 β-strands across 5 chains. 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: 14 helices, 26 β-strands

Element	Residues	Length	Sheet
β-strand	4-13	10	1
β-strand	16-26	11	1
β-strand	31-35	5	2
α-helix	42-50	9
β-strand	57-62	6	1
β-strand	65-66	2	1
α-helix	72-74	3
β-strand	77-80	4	2
α-helix	92-96	5
α-helix	98-101	4
α-helix	107-120	14
α-helix	131-133	3
α-helix	136-150	15
β-strand	154-158	5	2
α-helix	166-183	18
β-strand	186-190	5	2
α-helix	194-200	7
β-strand	203-208	6	2
β-strand	211-216	6	2
α-helix	218-223	6
β-strand	227	1	3
α-helix	228-233	6
α-helix	238-239	2
β-strand	240-249	10	4
β-strand	254-257	4	4
β-strand	265-268	4	4
β-strand	270	1	5
β-strand	280-285	6	4
α-helix	290	1
β-strand	291-292	2	6
β-strand	299-301	3	6
β-strand	303-309	7	7
β-strand	313-319	7	7
β-strand	327-332	6	7
β-strand	344-346	3	6
α-helix	349-351	3
β-strand	353-355	3	4
β-strand	360	1	3
β-strand	361	1	4
β-strand	364	1	5

Chain B: 15 helices, 25 β-strands

Element	Residues	Length	Sheet
β-strand	4-13	10	8
β-strand	16-25	10	8
β-strand	31-35	5	9
α-helix	42-50	9
β-strand	57-62	6	8
β-strand	66	1	8
α-helix	72-75	4
β-strand	77-80	4	9
α-helix	92-96	5
α-helix	99-103	5
α-helix	107-120	14
α-helix	131-133	3
α-helix	136-150	15
β-strand	154-158	5	9
α-helix	166-183	18
β-strand	186-190	5	9
α-helix	194-200	7
β-strand	203-208	6	9
β-strand	211-216	6	9
α-helix	218-223	6
β-strand	227	1	10
α-helix	228-233	6
α-helix	238-239	2
β-strand	240-249	10	11
β-strand	253-257	5	11
β-strand	265-269	5	11
β-strand	270	1	12
β-strand	280-285	6	11
α-helix	290	1
β-strand	291-292	2	13
β-strand	299-309	11	13
β-strand	313-319	7	13
β-strand	327-332	6	13
β-strand	342-346	5	13
α-helix	349-351	3
β-strand	353-355	3	11
β-strand	360	1	10
β-strand	361	1	11
α-helix	362-363	2
β-strand	364	1	12

Chain E: 22 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	6-10	5	14
α-helix	17-31	15
β-strand	34-38	5	14
α-helix	43-52	10
β-strand	59-63	5	14
α-helix	64-66	3
α-helix	67-72	6
β-strand	76	1	15
α-helix	77-79	3
α-helix	83-86	4
β-strand	89	1	16
α-helix	91-96	6
β-strand	98-99	2	17
β-strand	102-103	2	17
β-strand	105-111	7	14
β-strand	114-118	5	18
β-strand	128	1	19
α-helix	132-140	9
β-strand	145-147	3	18
α-helix	154-163	10
β-strand	167-171	5	20
β-strand	176-182	7	20
α-helix	186-200	15
α-helix	210-219	10
β-strand	222-227	6	18
α-helix	229-231	3
α-helix	232-238	7
β-strand	242-245	4	18
α-helix	246-248	3
β-strand	249-250	2	19
β-strand	253-254	2	19
α-helix	257	1
β-strand	258-259	2	21
β-strand	260-266	7	14
β-strand	267	1	15
α-helix	273-278	6
α-helix	279-284	6
α-helix	287-296	10
β-strand	301-302	2	14
β-strand	304	1	16
α-helix	305-311	7
α-helix	315-325	11
β-strand	328-329	2	21
α-helix	336-352	17
α-helix	357-368	12

Chain F: 31 helices, 23 β-strands

Element	Residues	Length	Sheet
α-helix	17-29	13
α-helix	31-35	5
α-helix	36-38	3
α-helix	40-57	18
α-helix	65-75	11
α-helix	76-80	5
α-helix	81-88	8
α-helix	89-91	3
β-strand	92	1	22
β-strand	100	1	23
α-helix	102-109	8
β-strand	113-115	3	24
β-strand	122-127	6	25
β-strand	130-136	7	25
β-strand	143-146	4	25
α-helix	147-148	2
β-strand	149	1	25
β-strand	155-158	4	26
β-strand	159-162	4	25
α-helix	165-166	2
α-helix	169-172	4
α-helix	173-178	6
α-helix	180-185	6
β-strand	186-189	4	26
β-strand	195-196	2	26
β-strand	197-198	2	27
β-strand	204-205	2	27
β-strand	207-209	3	24
β-strand	211-213	3	28
β-strand	219-221	3	28
β-strand	227-231	5	28
β-strand	236-240	5	28
β-strand	250-251	2	28
β-strand	255	1	23
β-strand	258	1	22
α-helix	266-268	3
α-helix	277-306	30
α-helix	314-320	7
α-helix	323-326	4
α-helix	329-339	11
α-helix	346-353	8
α-helix	365-391	27
α-helix	392-394	3
α-helix	398-405	8
α-helix	411-413	3
α-helix	414-418	5
α-helix	419-421	3
α-helix	423-438	16
α-helix	441-447	7
α-helix	451	1
β-strand	453	1	29
β-strand	462	1	29
α-helix	467-475	9
α-helix	484-503	20

Chain G: 17 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	10-39	30
β-strand	40	1	30
β-strand	54	1	30
α-helix	57-62	6
α-helix	81-112	32
α-helix	119-127	9
α-helix	136-150	15
α-helix	159-166	8
α-helix	171-181	11
α-helix	187-194	8
α-helix	199-201	3
α-helix	202-207	6
α-helix	208-227	20
α-helix	231-236	6
α-helix	240-242	3
α-helix	245-248	4
α-helix	249-252	4
β-strand	253	1	31
β-strand	258	1	31
α-helix	260-269	10
α-helix	271-281	11

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Maltose/maltodextrin import ATP-binding protein malK	A, B	protein	381	Escherichia coli	Q1R3Q1 (AlphaFold model)
Maltose-binding periplasmic protein	E	protein	370	Escherichia coli	P0AEX9 (AlphaFold model)
Maltose transport system permease protein malF	F	protein	514	Escherichia coli	P02916 (AlphaFold model)
Maltose transport system permease protein malG	G	protein	296	Escherichia coli	P68183 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>2R6G_1 Maltose/maltodextrin import ATP-binding protein malK (chains A, B)
MASVQLQNVTKAWGEVVVSKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDL
FIGEKRMNDTPPAERGVGMVFQSYALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEV
LQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDQPLSNLDAALRVQMRIEISRLH
KRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPADRFVAGFIGSPKMN
FLPVKVTATAIDQVQVELPMPNRQQVWLPVESRDVQVGANMSLGIRPEHLLPSDIADVIL
EGEVQVVEQLGNETQIHIQIPSIRQNLVYRQNDVVLVEEGATFAIGLPPERCHLFREDGT
ACRRLHKEPGVASASHHHHHH

Sequence of entity 2 (E), FASTA

>2R6G_2 Maltose-binding periplasmic protein (chains E)
KIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDII
FWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKD
LLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDIKD
VGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKV
NYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLG
AVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEA
LKDAQTRITK

Sequence of entity 3 (F), FASTA

>2R6G_3 Maltose transport system permease protein malF (chains F)
MDVIKKKHWWQSDALKWSVLGLLGLLVGYLVVLMYAQGEYLFAITTLILSSAGLYIFANR
KAYAWRYVYPGMAGMGLFVLFPLVCTIAIAFTNYSSTNQLTFERAQEVLLDRSWQAGKTY
NFGLYPAGDEWQLALSDGETGKNYLSDAFKFGGEQKLQLKETTAQPEGERANLRVITQNR
QALSDITAILPDGNKVMMSSLRQFSGTQPLYTLDGDGTLTNNQSGVKYRPNNQIGFYQSI
TADGNWGDEKLSPGYTVTTGWKNFTRVFTDEGIQKPFLAIFVWTVVFSLITVFLTVAVGM
VLACLVQWEALRGKAVYRVLLILPYAVPSFISILIFKGLFNQSFGEINMMLSALFGVKPA
WFSDPTTARTMLIIVNTWLGYPYMMILCMGLLKAIPDDLYEASAMDGAGPFQNFFKITLP
LLIKPLTPLMIASFAFNFNNFVLIQLLTNGGPDRLGTTTPAGYTDLLVNYTYRIAFEGGG
GQDFGLAAAIATLIFLLVGALAIVNLKATRMKFD

Sequence of entity 4 (G), FASTA

>2R6G_4 Maltose transport system permease protein malG (chains G)
MAMVQPKSQKARLFITHLLLLLFIAAIMFPLLMVVAISLRQGNFATGSLIPEQISWDHWK
LALGFSVEQADGRITPPPFPVLLWLWNSVKVAGISAIGIVALSTTCAYAFARMRFPGKAT
LLKGMLIFQMFPAVLSLVALYALFDRLGEYIPFIGLNTHGGVIFAYLGGIALHVWTIKGY
FETIDSSLEEAAALDGATPWQAFRLVLLPLSVPILAVVFILSFIAAITEVPVASLLLRDV
NSYTLAVGMQQYLNPQNYLWGDFAAAAVMSALPITIVFLLAQRWLVNGLTAGGVKG

Ligands and cofactors

ID	Name	Formula	Copies
ATP	Adenosine-5'-triphosphate	C10 H16 N5 O13 P3	2

Primary citation

Crystal structure of a catalytic intermediate of the maltose transporter. Oldham, M.L., Khare, D., Quiocho, F.A. et al. Nature (2007) 450:515-521. DOI 10.1038/nature06264 · PubMed

Browse structure collections

About this viewer

MolViewer shows 2R6G 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.