Anti-P24 (HIV-1) FAB fragment CB41 complexed with a peptide. Determined by X-ray diffraction at 2.6 Å resolution. Released 26 Jan 2001.
Explore 1HH6 in 3D Show helices and sheets RCSB PDB PDBe
1HH6 contains 16 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-7 | 4 | 1 |
| β-strand | 10-13 | 4 | 2 |
| β-strand | 19-25 | 7 | 1 |
| β-strand | 33-38 | 6 | 2 |
| β-strand | 45-49 | 5 | 2 |
| β-strand | 53-54 | 2 | 2 |
| α-helix | 55 | 1 | |
| β-strand | 62-66 | 5 | 1 |
| β-strand | 70-75 | 6 | 1 |
| α-helix | 80-82 | 3 | |
| β-strand | 84-90 | 7 | 2 |
| α-helix | 96 | 1 | |
| β-strand | 97-98 | 2 | 2 |
| β-strand | 102-106 | 5 | 2 |
| β-strand | 111 | 1 | 3 |
| β-strand | 114-118 | 5 | 4 |
| α-helix | 119-121 | 3 | |
| α-helix | 122-127 | 6 | |
| β-strand | 129-139 | 11 | 4 |
| β-strand | 140 | 1 | 3 |
| β-strand | 144-150 | 7 | 5 |
| β-strand | 153-155 | 3 | 5 |
| β-strand | 159-163 | 5 | 4 |
| β-strand | 173-182 | 10 | 4 |
| α-helix | 183-186 | 4 | |
| β-strand | 191-198 | 8 | 5 |
| β-strand | 201-210 | 10 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-6 | 4 | 6 |
| α-helix | 7-9 | 3 | |
| β-strand | 10-12 | 3 | 7 |
| β-strand | 18-25 | 8 | 6 |
| α-helix | 29-31 | 3 | |
| β-strand | 34-40 | 7 | 7 |
| β-strand | 44-51 | 8 | 7 |
| β-strand | 58-60 | 3 | 7 |
| α-helix | 62-64 | 3 | |
| β-strand | 65 | 1 | 6 |
| β-strand | 68-73 | 6 | 6 |
| α-helix | 74-76 | 3 | |
| β-strand | 78-83 | 6 | 6 |
| β-strand | 92-97 | 6 | 7 |
| β-strand | 102 | 1 | 7 |
| β-strand | 106-110 | 5 | 7 |
| α-helix | 113-115 | 3 | |
| β-strand | 116 | 1 | 8 |
| α-helix | 117-118 | 2 | |
| β-strand | 119-123 | 5 | 9 |
| α-helix | 124-126 | 3 | |
| β-strand | 134-144 | 11 | 9 |
| β-strand | 145 | 1 | 8 |
| β-strand | 150-153 | 4 | 10 |
| α-helix | 154-156 | 3 | |
| β-strand | 158 | 1 | 10 |
| β-strand | 162-164 | 3 | 9 |
| α-helix | 165-167 | 3 | |
| β-strand | 168-170 | 3 | 9 |
| β-strand | 173-183 | 11 | 9 |
| β-strand | 193-198 | 6 | 10 |
| α-helix | 199-201 | 3 | |
| β-strand | 203-208 | 6 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| IGG2A kappa antibody CB41 (light chain) | A | protein | 214 | MUS MUSCULUS | P01837 (AlphaFold model) |
| IGG2A kappa antibody CB41 (heavy chain) | B | protein | 213 | MUS MUSCULUS | P01864 (AlphaFold model) |
| PEP-4 | C | protein | 11 | synthetic construct |
>1HH6_1 IGG2A KAPPA ANTIBODY CB41 (LIGHT CHAIN) (chains A) DIKMTQSPSSMYTSLGERVTITCKASQDINSFLTWFLQKPGKSPKTLIYRANRLMIGVPS RFSGSGSGQTYSLTISSLEYEDMGIYYCLQYDDFPLTFGAGTKLDLKRADAAPTVSIFPP SSEQLTSGGASVVCFLNNFYPKEINVKWKIDGSERQNGVLDSWTEQDSKDSTYSMSSTLT LTKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC
>1HH6_2 IGG2A KAPPA ANTIBODY CB41 (HEAVY CHAIN) (chains B) QDQLQQSGAELVRPGASVKLSCKALGYIFTDYEIHWVKQTPVHGLEWIGGIHPGSSGTAY NQKFKGKATLTADKSSTTAFMELSSLTSEDSAVYYCTRKDYWGQGTLVTVSAAKTTAPSV YPLVPVCGGTTGSSVTLGCLVKGYFPEPVTLTWNSGSLSSGVHTFPALLQSGLYTLSSSV TVTSNTWPSQTITCNVAHPASSTKVDKKIEPRV
>1HH6_3 PEP-4 (chains C) DATPEDLGARL
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:
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