3RLF: Maltose-binding periplasmic protein
Crystal structure of the maltose-binding protein/maltose transporter complex in an outward-facing conformation bound to MgAMPPNP. Determined by X-ray diffraction at 2.2 Å resolution. Released 10 Aug 2011.
- Method
- X-ray diffraction
- Resolution
- 2.2 Å
- Organism
- Escherichia coli
- Chains
- 5
- Atoms
- 15,268
- Mol. weight
- 220.46 kDa
- Ligands
- PGV, MG, ANP, UMQ
- Released
- 10 Aug 2011
Explore 3RLF in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
3RLF contains 103 α-helices and 103 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: 17 helices, 25 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4-13 | 10 | 19 |
| β-strand | 16-26 | 11 | 19 |
| β-strand | 31-35 | 5 | 20 |
| α-helix | 42-50 | 9 | |
| β-strand | 57-62 | 6 | 19 |
| β-strand | 65-66 | 2 | 19 |
| α-helix | 72-74 | 3 | |
| β-strand | 77-80 | 4 | 20 |
| α-helix | 92-96 | 5 | |
| α-helix | 98-102 | 5 | |
| α-helix | 107-120 | 14 | |
| α-helix | 124-126 | 3 | |
| α-helix | 131-133 | 3 | |
| α-helix | 136-150 | 15 | |
| β-strand | 154-158 | 5 | 20 |
| α-helix | 166-183 | 18 | |
| β-strand | 186-190 | 5 | 20 |
| α-helix | 194-200 | 7 | |
| β-strand | 203-208 | 6 | 20 |
| β-strand | 211-216 | 6 | 20 |
| α-helix | 218-223 | 6 | |
| β-strand | 227 | 1 | 21 |
| α-helix | 228-233 | 6 | |
| α-helix | 238-239 | 2 | |
| β-strand | 240-249 | 10 | 22 |
| β-strand | 254-257 | 4 | 22 |
| β-strand | 265-268 | 4 | 22 |
| β-strand | 270 | 1 | 23 |
| β-strand | 280-285 | 6 | 22 |
| α-helix | 290 | 1 | |
| β-strand | 291-292 | 2 | 24 |
| α-helix | 293-295 | 3 | |
| β-strand | 299-309 | 11 | 24 |
| β-strand | 313-319 | 7 | 24 |
| α-helix | 326 | 1 | |
| β-strand | 327-332 | 6 | 24 |
| β-strand | 342-346 | 5 | 24 |
| α-helix | 349-351 | 3 | |
| β-strand | 353-355 | 3 | 22 |
| β-strand | 360 | 1 | 21 |
| β-strand | 361 | 1 | 22 |
| β-strand | 364 | 1 | 23 |
Chain B: 16 helices, 27 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4-13 | 10 | 25 |
| β-strand | 16-26 | 11 | 25 |
| β-strand | 31-35 | 5 | 26 |
| α-helix | 42-50 | 9 | |
| β-strand | 57-62 | 6 | 25 |
| β-strand | 66 | 1 | 25 |
| α-helix | 72-74 | 3 | |
| β-strand | 77-80 | 4 | 26 |
| α-helix | 92-104 | 13 | |
| α-helix | 107-120 | 14 | |
| α-helix | 131-133 | 3 | |
| α-helix | 136-150 | 15 | |
| β-strand | 154-158 | 5 | 26 |
| α-helix | 166-183 | 18 | |
| β-strand | 186-190 | 5 | 26 |
| α-helix | 194-200 | 7 | |
| β-strand | 203-208 | 6 | 26 |
| β-strand | 211-216 | 6 | 26 |
| α-helix | 218-223 | 6 | |
| β-strand | 227 | 1 | 27 |
| α-helix | 228-233 | 6 | |
| α-helix | 238-239 | 2 | |
| β-strand | 240-249 | 10 | 28 |
| β-strand | 254-257 | 4 | 28 |
| β-strand | 265-268 | 4 | 28 |
| β-strand | 270 | 1 | 29 |
| β-strand | 280-285 | 6 | 28 |
| α-helix | 290 | 1 | |
| β-strand | 291 | 1 | 30 |
| α-helix | 292 | 1 | |
| β-strand | 299 | 1 | 30 |
| β-strand | 303-309 | 7 | 31 |
| β-strand | 313-319 | 7 | 31 |
| α-helix | 326 | 1 | |
| β-strand | 327-332 | 6 | 31 |
| β-strand | 342 | 1 | 31 |
| β-strand | 346 | 1 | 30 |
| α-helix | 349-351 | 3 | |
| β-strand | 353-355 | 3 | 28 |
| β-strand | 360 | 1 | 27 |
| β-strand | 361 | 1 | 28 |
| α-helix | 362-363 | 2 | |
| β-strand | 364 | 1 | 29 |
Chain E: 22 helices, 26 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 2-3 | 2 | |
| β-strand | 7-10 | 4 | 1 |
| α-helix | 17-31 | 15 | |
| β-strand | 35-38 | 4 | 1 |
| α-helix | 43-51 | 9 | |
| β-strand | 59-63 | 5 | 1 |
| α-helix | 64-66 | 3 | |
| α-helix | 67-73 | 7 | |
| β-strand | 76 | 1 | 2 |
| α-helix | 77-79 | 3 | |
| α-helix | 83-86 | 4 | |
| β-strand | 89 | 1 | 3 |
| α-helix | 91-95 | 5 | |
| 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 | 132-140 | 9 | |
| β-strand | 145-147 | 3 | 5 |
| α-helix | 154-161 | 8 | |
| β-strand | 167 | 1 | 7 |
| β-strand | 171 | 1 | 8 |
| β-strand | 176 | 1 | 8 |
| β-strand | 182 | 1 | 7 |
| α-helix | 186-200 | 15 | |
| α-helix | 210-218 | 9 | |
| β-strand | 222-227 | 6 | 5 |
| α-helix | 229-231 | 3 | |
| α-helix | 232-238 | 7 | |
| β-strand | 242-245 | 4 | 5 |
| α-helix | 246-248 | 3 | |
| β-strand | 249 | 1 | 6 |
| β-strand | 250 | 1 | 9 |
| β-strand | 253 | 1 | 9 |
| β-strand | 258-259 | 2 | 10 |
| 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 | 315-325 | 11 | |
| β-strand | 328-329 | 2 | 10 |
| α-helix | 336-351 | 16 | |
| α-helix | 357-369 | 13 | |
Chain F: 29 helices, 19 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 14-29 | 16 | |
| α-helix | 31-35 | 5 | |
| α-helix | 40-58 | 19 | |
| α-helix | 60-62 | 3 | |
| α-helix | 65-75 | 11 | |
| α-helix | 76-80 | 5 | |
| α-helix | 81-89 | 9 | |
| β-strand | 92 | 1 | 11 |
| β-strand | 100 | 1 | 12 |
| α-helix | 102-111 | 10 | |
| β-strand | 113-127 | 15 | 13 |
| β-strand | 130-137 | 8 | 13 |
| β-strand | 142-146 | 5 | 13 |
| α-helix | 147-148 | 2 | |
| β-strand | 149 | 1 | 13 |
| β-strand | 155-162 | 8 | 13 |
| α-helix | 169-172 | 4 | |
| α-helix | 173-178 | 6 | |
| α-helix | 180-183 | 4 | |
| β-strand | 186-189 | 4 | 13 |
| β-strand | 195-198 | 4 | 13 |
| β-strand | 203-209 | 7 | 13 |
| β-strand | 211-213 | 3 | 14 |
| β-strand | 219-221 | 3 | 14 |
| β-strand | 227-231 | 5 | 14 |
| β-strand | 236-239 | 4 | 14 |
| β-strand | 250-251 | 2 | 14 |
| α-helix | 254 | 1 | |
| β-strand | 255 | 1 | 12 |
| β-strand | 258 | 1 | 11 |
| α-helix | 262-269 | 8 | |
| α-helix | 277-306 | 30 | |
| α-helix | 314-322 | 9 | |
| α-helix | 323-325 | 3 | |
| α-helix | 329-339 | 11 | |
| α-helix | 346-353 | 8 | |
| α-helix | 365-391 | 27 | |
| α-helix | 392-394 | 3 | |
| α-helix | 397-405 | 9 | |
| α-helix | 410-413 | 4 | |
| α-helix | 414-418 | 5 | |
| α-helix | 419-438 | 20 | |
| α-helix | 441-447 | 7 | |
| α-helix | 451 | 1 | |
| β-strand | 453 | 1 | 15 |
| β-strand | 462 | 1 | 15 |
| α-helix | 467-475 | 9 | |
| α-helix | 484-501 | 18 | |
Chain G: 19 helices, 6 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 12-38 | 27 | |
| β-strand | 40 | 1 | 16 |
| β-strand | 54 | 1 | 16 |
| α-helix | 57-62 | 6 | |
| α-helix | 65-66 | 2 | |
| β-strand | 67-68 | 2 | 17 |
| β-strand | 74-75 | 2 | 17 |
| α-helix | 81-112 | 32 | |
| α-helix | 118-129 | 12 | |
| α-helix | 136-148 | 13 | |
| α-helix | 152-154 | 3 | |
| α-helix | 159-166 | 8 | |
| α-helix | 171-181 | 11 | |
| α-helix | 187-194 | 8 | |
| α-helix | 199-202 | 4 | |
| α-helix | 203-207 | 5 | |
| 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 | 18 |
| β-strand | 258 | 1 | 18 |
| α-helix | 260-280 | 21 | |
| α-helix | 281-283 | 3 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Maltose-binding periplasmic protein | E | protein | 380 | 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) |
| Maltose/maltodextrin import ATP-binding protein MalK | A, B | protein | 381 | Escherichia coli | P68187 (AlphaFold model) |
Sequence of entity 1 (E), FASTA
>3RLF_1 Maltose-binding periplasmic protein (chains E)
KIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDII
FWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKD
LLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDIKD
VGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKV
NYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLG
AVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEA
LKDAQTRITKASASHHHHHH
Sequence of entity 2 (F), FASTA
>3RLF_2 Maltose transport system permease protein malF (chains F)
MDVIKKKHWWQSDALKWSVLGLLGLLVGYLVVLMYAQGEYLFAITTLILSSAGLYIFANR
KAYAWRYVYPGMAGMGLFVLFPLVCTIAIAFTNYSSTNQLTFERAQEVLLDRSWQAGKTY
NFGLYPAGDEWQLALSDGETGKNYLSDAFKFGGEQKLQLKETTAQPEGERANLRVITQNR
QALSDITAILPDGNKVMMSSLRQFSGTQPLYTLDGDGTLTNNQSGVKYRPNNQIGFYQSI
TADGNWGDEKLSPGYTVTTGWKNFTRVFTDEGIQKPFLAIFVWTVVFSLITVFLTVAVGM
VLACLVQWEALRGKAVYRVLLILPYAVPSFISILIFKGLFNQSFGEINMMLSALFGVKPA
WFSDPTTARTMLIIVNTWLGYPYMMILCMGLLKAIPDDLYEASAMDGAGPFQNFFKITLP
LLIKPLTPLMIASFAFNFNNFVLIQLLTNGGPDRLGTTTPAGYTDLLVNYTYRIAFEGGG
GQDFGLAAAIATLIFLLVGALAIVNLKATRMKFD
Sequence of entity 3 (G), FASTA
>3RLF_3 Maltose transport system permease protein malG (chains G)
MAMVQPKSQKARLFITHLLLLLFIAAIMFPLLMVVAISLRQGNFATGSLIPEQISWDHWK
LALGFSVEQADGRITPPPFPVLLWLWNSVKVAGISAIGIVALSTTCAYAFARMRFPGKAT
LLKGMLIFQMFPAVLSLVALYALFDRLGEYIPFIGLNTHGGVIFAYLGGIALHVWTIKGY
FETIDSSLEEAAALDGATPWQAFRLVLLPLSVPILAVVFILSFIAAITEVPVASLLLRDV
NSYTLAVGMQQYLNPQNYLWGDFAAAAVMSALPITIVFLLAQRWLVNGLTAGGVKG
Sequence of entity 4 (A, B), FASTA
>3RLF_4 Maltose/maltodextrin import ATP-binding protein MalK (chains A, B)
MASVQLQNVTKAWGEVVVSKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDL
FIGEKRMNDTPPAERGVGMVFQSYALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEV
LQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLH
KRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPADRFVAGFIGSPKMN
FLPVKVTATAIDQVQVELPMPNRQQVWLPVESRDVQVGANMSLGIRPEHLLPSDIADVIL
EGEVQVVEQLGNETQIHIQIPSIRQNLVYRQNDVVLVEEGATFAIGLPPERCHLFREDGT
ACRRLHKEPGVASASHHHHHH
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| PGV | (1R)-2-{[{[(2S)-2,3-dihydroxypropyl]oxy}(hydroxy)phosphoryl]oxy}-1-[(palmitoylo… | C40 H77 O10 P | 4 |
| MG | Magnesium ion | Mg | 2 |
| ANP | Phosphoaminophosphonic acid-adenylate ester | C10 H17 N6 O12 P3 | 2 |
| UMQ | Undecyl-maltoside | C23 H44 O11 | 1 |
Primary citation
Snapshots of the maltose transporter during ATP hydrolysis. Oldham, M.L., Chen, J. Proc Natl Acad Sci U S A (2011) 108:15152-15156. DOI 10.1073/pnas.1108858108 · 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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