Chimeric Affinity Matured Fab 7g12 complexed with mesoporphyrin. Determined by X-ray diffraction at 2.6 Å resolution. Released 4 Feb 2003.
Explore 1NGW in 3D Show helices and sheets RCSB PDB PDBe
1NGW contains 27 α-helices and 92 β-strands across 4 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 | 5-7 | 3 | 12 |
| β-strand | 10-14 | 5 | 13 |
| β-strand | 19-24 | 6 | 12 |
| β-strand | 30 | 1 | 14 |
| β-strand | 33-38 | 6 | 13 |
| β-strand | 45-49 | 5 | 13 |
| β-strand | 53-54 | 2 | 13 |
| α-helix | 55 | 1 | |
| β-strand | 62-67 | 6 | 12 |
| β-strand | 68 | 1 | 14 |
| β-strand | 70-75 | 6 | 12 |
| α-helix | 80-82 | 3 | |
| β-strand | 84-90 | 7 | 13 |
| α-helix | 96 | 1 | |
| β-strand | 97-98 | 2 | 13 |
| β-strand | 102-107 | 6 | 13 |
| β-strand | 111 | 1 | 15 |
| α-helix | 112-113 | 2 | |
| β-strand | 114-118 | 5 | 16 |
| α-helix | 119-121 | 3 | |
| α-helix | 122-126 | 5 | |
| β-strand | 130-139 | 10 | 16 |
| β-strand | 140 | 1 | 15 |
| β-strand | 144-150 | 7 | 17 |
| β-strand | 153-154 | 2 | 17 |
| β-strand | 159-163 | 5 | 16 |
| α-helix | 164-167 | 4 | |
| β-strand | 173-181 | 9 | 16 |
| α-helix | 183-188 | 6 | |
| β-strand | 191-198 | 8 | 17 |
| β-strand | 205-210 | 6 | 17 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-6 | 4 | 18 |
| β-strand | 10-12 | 3 | 19 |
| β-strand | 18-20 | 3 | 18 |
| β-strand | 22-25 | 4 | 18 |
| β-strand | 34-38 | 5 | 19 |
| β-strand | 46-51 | 6 | 19 |
| β-strand | 58-60 | 3 | 19 |
| β-strand | 68-73 | 6 | 18 |
| β-strand | 78-83 | 6 | 18 |
| α-helix | 88-90 | 3 | |
| β-strand | 92-98 | 7 | 19 |
| β-strand | 104 | 1 | 19 |
| β-strand | 108-112 | 5 | 19 |
| β-strand | 118 | 1 | 20 |
| α-helix | 119-120 | 2 | |
| β-strand | 121-125 | 5 | 21 |
| β-strand | 136-146 | 11 | 21 |
| β-strand | 147 | 1 | 20 |
| β-strand | 152-155 | 4 | 22 |
| α-helix | 156-158 | 3 | |
| β-strand | 160 | 1 | 22 |
| β-strand | 164-166 | 3 | 21 |
| α-helix | 167-169 | 3 | |
| β-strand | 170-171 | 2 | 21 |
| β-strand | 177-186 | 10 | 21 |
| α-helix | 187-189 | 3 | |
| β-strand | 195-201 | 7 | 22 |
| α-helix | 202-204 | 3 | |
| β-strand | 206-212 | 7 | 22 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 5-7 | 3 | 1 |
| β-strand | 10-14 | 5 | 2 |
| β-strand | 19-24 | 6 | 1 |
| β-strand | 30 | 1 | 3 |
| β-strand | 33-38 | 6 | 2 |
| β-strand | 45-49 | 5 | 2 |
| β-strand | 53-54 | 2 | 2 |
| α-helix | 55 | 1 | |
| β-strand | 62-65 | 4 | 1 |
| β-strand | 68 | 1 | 3 |
| 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 | 102-107 | 6 | 2 |
| β-strand | 111 | 1 | 4 |
| β-strand | 114-118 | 5 | 5 |
| α-helix | 119-121 | 3 | |
| α-helix | 122-126 | 5 | |
| β-strand | 130-139 | 10 | 5 |
| β-strand | 140 | 1 | 4 |
| β-strand | 144-150 | 7 | 6 |
| β-strand | 153-154 | 2 | 6 |
| β-strand | 159-163 | 5 | 5 |
| α-helix | 164-167 | 4 | |
| β-strand | 173-181 | 9 | 5 |
| α-helix | 183-188 | 6 | |
| β-strand | 191-198 | 8 | 6 |
| β-strand | 205-210 | 6 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Mature Metal Chelatase Catalytic Antibody, Light chain | A, L | protein | 213 | Mus musculus, Homo sapiens | |
| Mature Metal Chelatase Catalytic Antibody, Heavy chain | B, H | protein | 216 | Mus musculus, Homo sapiens | P06328 (AlphaFold model) |
>1NGW_1 Mature Metal Chelatase Catalytic Antibody, Light chain (chains A, L) ELVMTQTPKFMSTTVGDRVSITCKASQNVGTPVAWYQQKPGQSPKLLIYSASNRYTGVPD RFTGSGSGTDFTLTISNMQSEDLADYFCQQYSSYPLTFGGGTKVEIKRTVAAPSVFIFPP SDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLT LSKADYEKHKVYACEVTHQGLSSPVTKSFNRNE
>1NGW_2 Mature Metal Chelatase Catalytic Antibody, Heavy chain (chains B, H) QVQLLESGAELVKPGASVKLSCKASGYTFTSYWMHWVKQRPGRGLEWIGMIDPNSGGTKY NEKFKSKATLTVDKPSNTAYMQLSSLTSEDSAVYYCTRRDMDYWGAGTTVTVSSASTKGP SVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLS SVVTVPSSSLGTQTYICNVNHKPSNTKVDKKIVPKS
| ID | Name | Formula | Copies |
|---|---|---|---|
| MMP | N-methylmesoporphyrin | C35 H40 N4 O4 | 2 |
Structural evidence for substrate strain in antibody catalysis. Yin, J., Andryski, S.E., Beuscher IV, A.E. 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 P06328 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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