LolCDE(delta 235-252) complex with Pal lipoprotein. Determined by electron microscopy at 3.29 Å resolution. Released 21 Jan 2026.
Explore 9RLK in 3D Show helices and sheets RCSB PDB PDBe
9RLK contains 45 α-helices and 54 β-strands across 4 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 5-14 | 10 | |
| α-helix | 21-59 | 39 | |
| α-helix | 60-62 | 3 | |
| β-strand | 66-69 | 4 | 1 |
| β-strand | 75 | 1 | 2 |
| α-helix | 82-84 | 3 | |
| β-strand | 90-96 | 7 | 1 |
| β-strand | 99-104 | 6 | 3 |
| β-strand | 109-117 | 9 | 3 |
| α-helix | 126-128 | 3 | |
| β-strand | 129-130 | 2 | 3 |
| α-helix | 134-136 | 3 | |
| β-strand | 143-147 | 5 | 3 |
| α-helix | 148-154 | 7 | |
| β-strand | 160-161 | 2 | 3 |
| β-strand | 163-166 | 4 | 3 |
| β-strand | 180-182 | 3 | 3 |
| β-strand | 185-190 | 6 | 3 |
| α-helix | 195-198 | 4 | |
| β-strand | 200-204 | 5 | 3 |
| α-helix | 205-211 | 7 | |
| α-helix | 214-215 | 2 | |
| β-strand | 219 | 1 | 2 |
| β-strand | 221-226 | 6 | 1 |
| α-helix | 234-237 | 4 | |
| α-helix | 240-241 | 2 | |
| β-strand | 245-248 | 4 | 1 |
| α-helix | 250-303 | 54 | |
| α-helix | 307-347 | 41 | |
| α-helix | 362-389 | 28 | |
| α-helix | 392-396 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 6-9 | 4 | 8 |
| β-strand | 14-15 | 2 | 9 |
| β-strand | 22-23 | 2 | 9 |
| β-strand | 31-32 | 2 | 8 |
| β-strand | 37-41 | 5 | 10 |
| α-helix | 50-55 | 6 | |
| β-strand | 65-68 | 4 | 8 |
| β-strand | 72 | 1 | 8 |
| α-helix | 73-75 | 3 | |
| α-helix | 78-88 | 11 | |
| β-strand | 90-93 | 4 | 10 |
| α-helix | 104-114 | 11 | |
| α-helix | 119-133 | 15 | |
| α-helix | 149-160 | 12 | |
| β-strand | 166-170 | 5 | 10 |
| α-helix | 178-194 | 17 | |
| β-strand | 198-203 | 6 | 10 |
| β-strand | 214-218 | 5 | 10 |
| β-strand | 223-224 | 2 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 5-15 | 11 | |
| α-helix | 23-58 | 36 | |
| β-strand | 67-68 | 2 | 4 |
| α-helix | 78-86 | 9 | |
| β-strand | 91 | 1 | 5 |
| β-strand | 96-97 | 2 | 4 |
| β-strand | 98-99 | 2 | 6 |
| β-strand | 102-103 | 2 | 7 |
| β-strand | 112-113 | 2 | 7 |
| β-strand | 114-118 | 5 | 6 |
| α-helix | 120-126 | 7 | |
| α-helix | 129-132 | 4 | |
| β-strand | 133 | 1 | 6 |
| β-strand | 147-151 | 5 | 6 |
| α-helix | 152-158 | 7 | |
| β-strand | 166-170 | 5 | 7 |
| β-strand | 183-187 | 5 | 7 |
| β-strand | 188-193 | 6 | 6 |
| α-helix | 198-202 | 5 | |
| β-strand | 203-207 | 5 | 6 |
| α-helix | 208-214 | 7 | |
| β-strand | 223-225 | 3 | 4 |
| β-strand | 228 | 1 | 5 |
| α-helix | 239-281 | 43 | |
| α-helix | 283-292 | 10 | |
| α-helix | 296-327 | 32 | |
| α-helix | 329-340 | 12 | |
| α-helix | 361-387 | 27 | |
| α-helix | 391-396 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-9 | 6 | 11 |
| β-strand | 13-15 | 3 | 12 |
| β-strand | 22-25 | 4 | 12 |
| β-strand | 31-33 | 3 | 11 |
| β-strand | 37-41 | 5 | 13 |
| α-helix | 50-55 | 6 | |
| β-strand | 65-68 | 4 | 11 |
| β-strand | 72 | 1 | 11 |
| α-helix | 73-75 | 3 | |
| α-helix | 78-88 | 11 | |
| β-strand | 90-92 | 3 | 13 |
| α-helix | 104-114 | 11 | |
| α-helix | 119-133 | 15 | |
| α-helix | 150-160 | 11 | |
| β-strand | 166-170 | 5 | 13 |
| α-helix | 178-195 | 18 | |
| β-strand | 198-202 | 5 | 13 |
| α-helix | 208-210 | 3 | |
| β-strand | 214-218 | 5 | 13 |
| β-strand | 223-224 | 2 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Lipoprotein-releasing system transmembrane protein LolC | C | protein | 399 | Escherichia coli K-12 | P0ADC3 (AlphaFold model) |
| Lipoprotein-releasing system transmembrane protein LolE | E | protein | 398 | Escherichia coli K-12 | P75958 (AlphaFold model) |
| Lipoprotein-releasing system ATP-binding protein LolD | D, F | protein | 241 | Escherichia coli K-12 | P75957 (AlphaFold model) |
| Peptidoglycan-associated lipoprotein | P | protein | 162 | Escherichia coli K-12 | P0A912 (AlphaFold model) |
>9RLK_1 Lipoprotein-releasing system transmembrane protein LolC (chains C) MYQPVALFIGLRYMRGRAADRFGRFVSWLSTIGITLGVMALVTVLSVMNGFERELQNNIL GLMPQAILSSEHGSLNPQQLPETAVKLDGVNRVAPITTGDVVLQSARSVAVGVMLGIDPA QKDPLTPYLVNVKQTDLEPGKYNVILGEQLASQLGVNRGDQIRVMVPSASQFTPMGRIPS QRLFNVIGTFAANSEVDGYEMLVNIEDASRLMRYPAGNITGWRLWLDEPLKVDSLSQQKL PEGSKWQDWRDRKGELFQAVRMEKNMMGLLLSLIVAVAAFNIITSLGLMVMEKQGEVAIL QTQGLTPRQIMMVFMVQGASAGIIGAILGAALGALLASQLNNLMPIIGVLLDGAALPVAI EPLQVIVIALVAMAIALLSTLYPSWRAAATQPAEALRYE
>9RLK_2 Lipoprotein-releasing system transmembrane protein LolE (chains E) MAMPLSLLIGLRFSRGRRRGGMVSLISVISTIGIALGVAVLIVGLSAMNGFERELNNRIL AVVPHGEIEAVDQPWTNWQEALDHVQKVPGIAAAAPYINFTGLVESGANLRAIQVKGVNP QQEQRLSALPSFVQGDAWRNFKAGEQQIIIGKGVADALKVKQGDWVSIMIPNSNPEHKLM QPKRVRLHVAGILQLSGQLDHSFAMIPLADAQQYLDMGSSVSGIALKMTDVFNAGSSWIG TYGYMYRDIQMIRAIMYLAMVLVIGVACFNIVSTLVMAVKDKSGDIAVLRTLGAKDGLIR AIFVWYGLLAGLFGSLCGVIIGVVVSLQLTPIIEWIEKLIGHQFLSSDIYFIDFLPSELH WLDVFYVLVTALLLSLLASWYPARRASNIDPARVLSGQ
>9RLK_3 Lipoprotein-releasing system ATP-binding protein LolD (chains D, F) MNKILLQCDNLCKRYQEGSVQTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDT PTSGDVIFNGQPMSKLSSAAKAELRNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPA EINSRALEMLKAVGLDHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARN ADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAELSLMGAEGSHHHHH H
>9RLK_4 Peptidoglycan-associated lipoprotein (chains P) CSSNKNASNDGSEGMLGAGTGMDANGGNGNMSSEEQARLQMQQLQQNNIVYFDLDKYDIR SDFAQMLDAHANFLRSNPSYKVTVEGHADERGTPEYNISLGERRANAVKMYLQGKGVSAD QISIVSYGKEKPAVLGHDEAAYSKNRRAVLVYGSWSHPQFEK
| ID | Name | Formula | Copies |
|---|---|---|---|
| Z41 | (2S)-3-hydroxypropane-1,2-diyl dihexadecanoate | C35 H68 O5 | 1 |
| PLM | Palmitic acid | C16 H32 O2 | 1 |
Liganded LolCDE structures reveal a common substrate-LolE interaction guiding bacterial lipoprotein transport. Szewczyk, P., Greene, N.P., Symmons, M.F. et al. Proc Natl Acad Sci U S A (2026) 123:e2520579123-e2520579123. DOI 10.1073/pnas.2520579123 · PubMed
Other PDB entries of the same protein (UniProt P0ADC3 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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