7RAH: Adenylate cyclase toxin RTX domain fragment

Adenylate cyclase toxin RTX domain fragment bound to M1H5 Fab and M2B10 Fab. Determined by X-ray diffraction at 2.6 Å resolution. Released 15 Sept 2021.

Method
X-ray diffraction
Resolution
2.6 Å
Organisms
Mus musculus, Bordetella pertussis
Chains
5
Atoms
9,183
Mol. weight
146.49 kDa
Ligands
CA, PO4
Released
15 Sept 2021

Explore 7RAH in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7RAH contains 32 α-helices and 124 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: 6 helices, 21 β-strands

ElementResiduesLengthSheet
β-strand4-521
β-strand10-1342
β-strand19-2571
β-strand33-3862
β-strand44-4962
β-strand53-5422
α-helix551
β-strand62-6761
β-strand70-7561
α-helix80-823
β-strand84-9072
β-strand9812
β-strand102-10652
β-strand11213
β-strand115-11954
α-helix120-1223
α-helix123-1286
β-strand130-140114
β-strand14113
β-strand146-15165
β-strand154-15635
β-strand160-16454
α-helix165-1684
β-strand174-183104
α-helix184-1874
β-strand192-19985
β-strand202-211105
Chain B: 10 helices, 23 β-strands
ElementResiduesLengthSheet
β-strand3-756
β-strand11-1227
β-strand18-2586
α-helix29-313
β-strand34-3968
β-strand45-5178
β-strand57-5828
β-strand67-7266
β-strand77-8266
α-helix84-863
β-strand88-98118
β-strand100A-10378
β-strand107-10938
β-strand110-11127
α-helix115-1162
β-strand11719
α-helix118-1192
β-strand120-124510
α-helix128-1303
β-strand131-132210
β-strand135-1451110
β-strand14619
β-strand151-154411
α-helix155-1573
β-strand163-165310
α-helix166-1683
β-strand169-170210
β-strand176-1851010
α-helix186-1905
β-strand194-200711
α-helix201-2033
β-strand205-211711
α-helix212-2143
Chain C: 6 helices, 20 β-strands
ElementResiduesLengthSheet
β-strand4-7412
β-strand10-13413
β-strand19-25712
α-helix30-323
β-strand33-38613
β-strand45-49513
β-strand53-54213
β-strand62-67612
β-strand70-75612
α-helix80-823
β-strand84-90713
α-helix961
β-strand97-98213
β-strand102-106513
β-strand111114
β-strand114-118515
α-helix119-1213
α-helix122-1254
β-strand133-139715
β-strand140114
β-strand144-147416
β-strand161-163315
α-helix164-1674
β-strand173-177515
β-strand195-198416
β-strand205-206216
Chain D: 5 helices, 24 β-strands
ElementResiduesLengthSheet
β-strand3-6417
α-helix71
β-strand10-12318
β-strand18-25817
α-helix29-313
β-strand32-39818
β-strand46-51618
β-strand57-59318
α-helix61-633
β-strand64117
β-strand67-72617
β-strand77-82617
α-helix84-863
β-strand88-971018
β-strand102-103218
β-strand107-111518
β-strand121119
β-strand136-139420
β-strand142-145419
β-strand150-153421
β-strand154122
β-strand159122
β-strand163-165320
α-helix166-1683
β-strand169-170219
β-strand176-178319
β-strand180-184520
β-strand197-200421
β-strand205-208421
Chain E: 5 helices, 36 β-strands
ElementResiduesLengthSheet
β-strand1057-1059323
β-strand1066-1068324
β-strand1076-1079423
β-strand1086-1088324
α-helix1093-10953
α-helix1096-11027
β-strand1105-1110623
β-strand1115-1117323
β-strand1127-1131523
β-strand1135-1137324
β-strand1142-1146523
β-strand1153-1155324
β-strand1162-1164323
β-strand1171-1173324
β-strand1180-1182323
β-strand1189-1191324
β-strand1200-1202323
β-strand1209-1211324
α-helix1213-12153
β-strand1225123
β-strand1229-1234623
β-strand1239-1245723
β-strand1248-1255823
β-strand1259-1261324
β-strand1266-1270523
β-strand1277-1279324
β-strand1286-1288323
β-strand1295-1297324
β-strand1304-1306323
β-strand1313-1315324
β-strand1322-1324323
β-strand1342-1344324
β-strand1351-1354423
β-strand1360-1363424
β-strand1372-1375423
α-helix1379-13813
β-strand1382-1387624
β-strand1390-1395624
β-strand1401-1404424
α-helix1411-14133
β-strand1417-1420423

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
M1H5 Fab Light ChainAprotein215Mus musculus
M1H5 Fab Heavy ChainBprotein233Mus musculus
M2B10 Fab Light ChainCprotein214Mus musculus
M2B10 Fab Heavy ChainDprotein235Mus musculus
Bifunctional adenylate cyclase toxin/hemolysin CyaA,Bifunctional adenylate cyclase toxin/hemolysin…Eprotein458Bordetella pertussisP0DKX7 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>7RAH_1 M1H5 Fab Light Chain (chains A)
DIQMIQSTSSLSASLGDRVTISCRASQDISNYLNWYQQKPDGTVKLLIYYTSRLHSGVPS
RFSGSGSGTDYSLTISNLEQEDIATYFCQQGNTLPYTFGGGTKLEIKRTADAAPTVSIFP
PSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMSSTL
TLTKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC
Sequence of entity 2 (B), FASTA
>7RAH_2 M1H5 Fab Heavy Chain (chains B)
EVNLVESGGDLVKPGGSLKLSCAASGFTFSSYGMSWVRQTPDKRLEWVATISSGGTYTYY
PDSVKGRFTISRDNAKNTLYLQMSSLKSEDTAMYYCAREIMRGGGYYFDYWSQGTTLTVS
SRSTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQS
SGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKGLEVLFQ
Sequence of entity 3 (C), FASTA
>7RAH_3 M2B10 Fab Light Chain (chains C)
IVMTQSPAILSASLGERVTMTCTASSSVSSSYLHWYQQKPGSSPKLWIYSTSNLASGVPA
RFSGSGSGTSYSLTISSMEAEDAATYYCHQYHRSPPTFGAGTKLEIKRTVAAPSVFIFPP
SDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLT
LSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
Sequence of entity 4 (D), FASTA
>7RAH_4 M2B10 Fab Heavy Chain (chains D)
EVQLQQSGAELVRPGTSVKVSCKASGYAFTNYLIEWVKQRPGQGLEWIGVINPGIGNTNY
NEKFKGKATLTADKSSSTVYMQLSSLTSDDSAVYFCARGLNYGSSQHWYFDVWGAGTSVT
VSSRSTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVL
QSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKGLEVLFQ
Sequence of entity 5 (E), FASTA
>7RAH_5 Bifunctional adenylate cyclase toxin/hemolysin CyaA,Bifunctional adenylate cyclase toxin/hemolysin CyaA (chains E)
GPGSGGAGNDSITGNAHDNFLAGGSGDDRLDGGAGNDTLVGGEGQNTVIGGAGDDVFLQD
LGVWSNQLDGGAGVDTVKYNVHQPSEERLERMGDTGIHADLQKGTVEKWPALNLFSVDHV
KNIENLHGSRLNDRIAGDDQDNELWGHDGNDTIRGRGGDDILRGGLGLDTLYGEDGNDIF
LQDDETVSDDIDGGAGLDTVDYSAMIHPGRIVAPHEYGFGIEADLSREWVRKASALGVDY
YDNVRNVENVIGTSMKDVLIGDAQANTLMGQGGDDTVRGGDGDDLLFGGDGNDMLYGDAG
NDTLYGGLGDDTLEGGAGNDWFGQTQAREHDVLRGGDGVDTYLFGVGYGHDTIYESGGGH
DTIRINAGADQLWFARQGNDLEIRILGTDDALTVHDWYRDADHRVEIIHAANQAVDQAGI
EKLVEAMAQYPDPGAAAAAPPAARVPDTLMQSLAVNWR

Ligands and cofactors

IDNameFormulaCopies
CACalcium ionCa19
PO4Phosphate ionO4 P1

Primary citation

Structural basis for antibody binding to adenylate cyclase toxin reveals RTX linkers as neutralization-sensitive epitopes. Goldsmith, J.A., DiVenere, A.M., Maynard, J.A. et al. PLoS Pathog (2021) 17:e1009920-e1009920. DOI 10.1371/journal.ppat.1009920 · PubMed

Other PDB entries of the same protein (UniProt P0DKX7 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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