PFA1 FAB complexed with GripI peptide fragment. Determined by X-ray diffraction at 2.1 Å resolution. Released 16 Oct 2007.
Explore 2R0Z in 3D Show helices and sheets RCSB PDB PDBe
2R0Z contains 17 α-helices and 47 β-strands across 3 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 | 3-7 | 5 | 8 |
| β-strand | 11-12 | 2 | 9 |
| α-helix | 17 | 1 | |
| β-strand | 18-25 | 8 | 8 |
| β-strand | 34-39 | 8 | 10 |
| β-strand | 46-52 | 7 | 10 |
| β-strand | 57-59 | 3 | 10 |
| α-helix | 61-63 | 3 | |
| β-strand | 67-72 | 6 | 8 |
| β-strand | 77-82 | 6 | 8 |
| α-helix | 84-86 | 3 | |
| β-strand | 88-96 | 9 | 10 |
| β-strand | 103 | 1 | 10 |
| β-strand | 107-109 | 3 | 10 |
| β-strand | 110-111 | 2 | 9 |
| β-strand | 117 | 1 | 11 |
| α-helix | 118-119 | 2 | |
| β-strand | 120-124 | 5 | 12 |
| α-helix | 125-127 | 3 | |
| β-strand | 135-145 | 11 | 12 |
| β-strand | 146 | 1 | 11 |
| β-strand | 151-155 | 5 | 13 |
| β-strand | 162-165 | 4 | 12 |
| α-helix | 166-168 | 3 | |
| β-strand | 169-170 | 2 | 12 |
| β-strand | 175-184 | 10 | 12 |
| α-helix | 185-187 | 3 | |
| β-strand | 194-199 | 6 | 13 |
| α-helix | 200-202 | 3 | |
| β-strand | 204-209 | 6 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-7 | 4 | 1 |
| β-strand | 10-13 | 4 | 2 |
| β-strand | 19-25 | 7 | 1 |
| β-strand | 27C | 1 | 3 |
| β-strand | 31 | 1 | 3 |
| β-strand | 33-38 | 6 | 2 |
| α-helix | 43-44 | 2 | |
| β-strand | 45-49 | 5 | 2 |
| β-strand | 53-54 | 2 | 2 |
| β-strand | 62-67 | 6 | 1 |
| β-strand | 70-75 | 6 | 1 |
| α-helix | 80-82 | 3 | |
| β-strand | 84-90 | 7 | 2 |
| β-strand | 93 | 1 | 4 |
| α-helix | 96 | 1 | |
| β-strand | 97-98 | 2 | 2 |
| β-strand | 102-106 | 5 | 2 |
| β-strand | 110 | 1 | 5 |
| α-helix | 111-112 | 2 | |
| β-strand | 113-117 | 5 | 6 |
| α-helix | 118-120 | 3 | |
| α-helix | 121-125 | 5 | |
| β-strand | 128-138 | 11 | 6 |
| β-strand | 139 | 1 | 5 |
| β-strand | 143-149 | 7 | 7 |
| β-strand | 152-154 | 3 | 7 |
| β-strand | 158-162 | 5 | 6 |
| α-helix | 163-166 | 4 | |
| β-strand | 172-181 | 10 | 6 |
| α-helix | 182-185 | 4 | |
| β-strand | 190-197 | 8 | 7 |
| β-strand | 204-209 | 6 | 7 |
| α-helix | 210-212 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3 | 1 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| IgG2a Fab fragment light chain | L | protein | 219 | Mus musculus | A2NHM3 (AlphaFold model) |
| IgG2a Fab fragment heavy chain, Fd portion | H | protein | 223 | Mus musculus | P01863 (AlphaFold model) |
| GripI peptide fragment | Q | protein | 6 |
>2R0Z_1 IgG2a Fab fragment light chain (chains L) DVLMTQTPLSLPVSLGDQASISCRSSQSIVHSNGNTYLEWYLQKPGQSPKLLIYKVSNRF SGVPDRFSGSGSGTDFTLKISRVEAEDLGVYYCFQGSHVPLTFGAGTKLELKRADAAPTV SIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSM SSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC
>2R0Z_2 IgG2a Fab fragment heavy chain, Fd portion (chains H) QVTLKESGPGILKPSQTLSLTCSFSGFSLSTSGMGVGWIRQPSGKGLEWLAHIWWDDDRS YNPSLKSQLTISKDTSRNQVFLRITSVDTADTATYYCVRRAHTTVLGDWFAYWGQGTLVT VSAAKTTAPSVYPLAPVCGDTTGSSVTLGCLVKGYFPEPVTLTWNSGSLSSGVHTFPALL QSDLYTLSSSSTVTSSTWPSQSITCNVAHPASSTKVDKKIEPR
>2R0Z_3 GripI peptide fragment (chains Q) AKFRHD
Molecular basis for passive immunotherapy of Alzheimer's disease. Gardberg, A.S., Dice, L.T., Ou, S. et al. Proc Natl Acad Sci U S A (2007) 104:15659-15664. DOI 10.1073/pnas.0705888104 · PubMed
Other PDB entries of the same protein (UniProt A2NHM3 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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