Chimeric Germline Fab 7g12-apo. Determined by X-ray diffraction at 1.6 Å resolution. Released 4 Feb 2003.
Explore 1NGZ in 3D Show helices and sheets RCSB PDB PDBe
1NGZ contains 17 α-helices and 42 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 |
| α-helix | 112-113 | 2 | |
| β-strand | 114-118 | 5 | 4 |
| α-helix | 119-121 | 3 | |
| α-helix | 122-125 | 4 | |
| β-strand | 129-139 | 11 | 4 |
| β-strand | 140 | 1 | 3 |
| β-strand | 145-150 | 6 | 5 |
| β-strand | 153-154 | 2 | 5 |
| α-helix | 155 | 1 | |
| β-strand | 159-163 | 5 | 4 |
| α-helix | 164-167 | 4 | |
| β-strand | 173-182 | 10 | 4 |
| α-helix | 183-188 | 6 | |
| β-strand | 191-197 | 7 | 5 |
| β-strand | 205-210 | 6 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-6 | 4 | 6 |
| β-strand | 9-12 | 4 | 2 |
| β-strand | 18-25 | 8 | 6 |
| β-strand | 34-39 | 6 | 2 |
| β-strand | 46-51 | 6 | 2 |
| β-strand | 58-60 | 3 | 2 |
| α-helix | 62-64 | 3 | |
| β-strand | 68-73 | 6 | 6 |
| α-helix | 74-76 | 3 | |
| β-strand | 78-83 | 6 | 6 |
| α-helix | 88-90 | 3 | |
| β-strand | 92-97 | 6 | 2 |
| β-strand | 108-112 | 5 | 2 |
| β-strand | 118 | 1 | 7 |
| α-helix | 119-120 | 2 | |
| β-strand | 121-125 | 5 | 8 |
| β-strand | 136-146 | 11 | 8 |
| β-strand | 147 | 1 | 7 |
| β-strand | 152-155 | 4 | 9 |
| α-helix | 156-158 | 3 | |
| β-strand | 160 | 1 | 9 |
| β-strand | 164-166 | 3 | 8 |
| α-helix | 167-169 | 3 | |
| β-strand | 170-171 | 2 | 8 |
| β-strand | 177-186 | 10 | 8 |
| α-helix | 187-189 | 3 | |
| β-strand | 195-201 | 7 | 9 |
| α-helix | 202-204 | 3 | |
| β-strand | 206-212 | 7 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Germline Metal Chelatase Catalytic Antibody, Light chain | A | protein | 213 | Mus musculus, Homo sapiens | P01834 (AlphaFold model) |
| Germline Metal Chelatase Catalytic Antibody, Heavy chain | B | protein | 220 | Mus musculus, Homo sapiens | P06328 (AlphaFold model) |
>1NGZ_1 Germline Metal Chelatase Catalytic Antibody, Light chain (chains A) ELVMTQTPKFMSTSVGDRVSITCKASQNVGTAVAWYQQKPGQSPKLLIYSASNRYTGVPD RFTGSGSGTDFTLTISNMQSEDLADYFCQQYSSYPLTFGGGTKVEIKRTVAAPSVFIFPP SDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLT LSKADYEKHKVYACEVTHQGLSSPVTKSFNRGE
>1NGZ_2 Germline Metal Chelatase Catalytic Antibody, Heavy chain (chains B) QVQLLESGAELVKPGASVKLSCKASGYTFTSYWMHWVKQRPGRGLEWIGRIDPNSGGTKY NEKFKSKATLTVDKPSSTAYMQLSSLTSEDSAVYYCTRRDSDYWGAGTTVTVSSASTKGP SVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLS SVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKT
Structural evidence for substrate strain in antibody catalysis. Yin, J., Andryski, S.A., Beuscher, A.B. et al. Proc Natl Acad Sci U S A (2003) 100:856-861. DOI 10.1073/pnas.0235873100 · PubMed
Other PDB entries of the same protein (UniProt P01834 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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