1HH9: Anti-P24 (HIV-1) FAB fragment CB41

Anti-P24 (HIV-1) FAB fragment CB41 complexed with a peptide. Determined by X-ray diffraction at 2.7 Å resolution. Released 12 Jan 2001.

Method
X-ray diffraction
Resolution
2.7 Å
Organisms
MUS MUSCULUS, synthetic construct
Chains
3
Atoms
3,401
Mol. weight
47.78 kDa
Released
12 Jan 2001

Explore 1HH9 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1HH9 contains 15 α-helices and 44 β-strands across 2 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: 9 helices, 21 β-strands

ElementResiduesLengthSheet
β-strand4-741
β-strand10-1342
β-strand19-2571
β-strand33-3862
α-helix43-442
β-strand45-4952
β-strand53-5422
α-helix551
β-strand62-6651
β-strand70-7561
α-helix80-823
β-strand84-9072
α-helix961
β-strand97-9822
β-strand102-10652
β-strand11113
β-strand114-11854
α-helix119-1213
α-helix122-1254
β-strand129-139114
β-strand14013
β-strand144-15075
β-strand153-15535
β-strand159-16354
α-helix165-1673
β-strand173-182104
α-helix183-1864
β-strand191-19885
β-strand201-210105
α-helix211-2133
Chain B: 6 helices, 23 β-strands
ElementResiduesLengthSheet
β-strand3-646
α-helix7-93
β-strand10-1237
β-strand18-2586
β-strand34-4077
β-strand44-5297
β-strand57-6047
α-helix62-643
β-strand6516
β-strand68-7366
β-strand78-8366
β-strand92-9767
β-strand10217
β-strand106-11057
α-helix113-1153
β-strand11618
α-helix117-1182
β-strand119-12359
β-strand134-144119
β-strand14518
β-strand151-153310
α-helix154-1563
β-strand158110
β-strand162-16439
α-helix165-1673
β-strand168-17039
β-strand173-183119
β-strand193-198610
β-strand203-208610

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
IGG2A kappa antibody CB41 (light chain)Aprotein214MUS MUSCULUSP01837 (AlphaFold model)
IGG2A kappa antibody CB41 (heavy chain)Bprotein213MUS MUSCULUSP01864 (AlphaFold model)
PEP-2Cprotein12synthetic construct
Sequence of entity 1 (A), FASTA
>1HH9_1 IGG2A KAPPA ANTIBODY CB41 (LIGHT CHAIN) (chains A)
DIKMTQSPSSMYTSLGERVTITCKASQDINSFLTWFLQKPGKSPKTLIYRANRLMIGVPS
RFSGSGSGQTYSLTISSLEYEDMGIYYCLQYDDFPLTFGAGTKLDLKRADAAPTVSIFPP
SSEQLTSGGASVVCFLNNFYPKEINVKWKIDGSERQNGVLDSWTEQDSKDSTYSMSSTLT
LTKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC
Sequence of entity 2 (B), FASTA
>1HH9_2 IGG2A KAPPA ANTIBODY CB41 (HEAVY CHAIN) (chains B)
QDQLQQSGAELVRPGASVKLSCKALGYIFTDYEIHWVKQTPVHGLEWIGGIHPGSSGTAY
NQKFKGKATLTADKSSTTAFMELSSLTSEDSAVYYCTRKDYWGQGTLVTVSAAKTTAPSV
YPLVPVCGGTTGSSVTLGCLVKGYFPEPVTLTWNSGSLSSGVHTFPALLQSGLYTLSSSV
TVTSNTWPSQTITCNVAHPASSTKVDKKIEPRV
Sequence of entity 3 (C), FASTA
>1HH9_3 PEP-2 (chains C)
DATPEDLNAKLX

Primary citation

Evolutionary Transition Pathways for Changing Peptide Ligand Specificity and Structure. Hoffmuller, U., Knaute, T., Hahn, M. et al. EMBO J (2000) 19:4866. DOI 10.1093/EMBOJ/19.18.4866 · PubMed

Other PDB entries of the same protein (UniProt P01837 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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