Complement factor D in complex with the inhibitor 2-(2-(3'-(aminomethyl)-[1,1'-biphenyl]-3-carboxamido)phenyl)acetic acid. Determined by X-ray diffraction at 1.8 Å resolution. Released 24 Apr 2019.
Explore 6QMT in 3D Show helices and sheets RCSB PDB PDBe
6QMT contains 19 α-helices and 40 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 | 17 | 1 | 1 |
| β-strand | 20-21 | 2 | 2 |
| α-helix | 22-23 | 2 | |
| β-strand | 30-35 | 6 | 3 |
| β-strand | 39-48 | 10 | 3 |
| β-strand | 51-54 | 4 | 3 |
| α-helix | 56-60 | 5 | |
| β-strand | 64-68 | 5 | 3 |
| β-strand | 72 | 1 | 4 |
| β-strand | 81-90 | 10 | 3 |
| β-strand | 104-108 | 5 | 3 |
| α-helix | 111-114 | 4 | |
| β-strand | 115 | 1 | 5 |
| β-strand | 120 | 1 | 5 |
| β-strand | 124A | 1 | 2 |
| α-helix | 129A-131 | 3 | |
| β-strand | 135-140 | 6 | 2 |
| α-helix | 150-152 | 3 | |
| β-strand | 154 | 1 | 4 |
| β-strand | 156-163 | 8 | 2 |
| α-helix | 164 | 1 | |
| α-helix | 165-169 | 5 | |
| β-strand | 180-183 | 4 | 2 |
| β-strand | 189 | 1 | 1 |
| β-strand | 198-201 | 4 | 2 |
| β-strand | 208-213 | 6 | 2 |
| β-strand | 226-230 | 5 | 2 |
| α-helix | 231-234 | 4 | |
| α-helix | 235-242 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 17 | 1 | 6 |
| β-strand | 20-21 | 2 | 7 |
| α-helix | 22-23 | 2 | |
| β-strand | 30-35 | 6 | 8 |
| β-strand | 39-48 | 10 | 8 |
| β-strand | 51-54 | 4 | 8 |
| α-helix | 57-60 | 4 | |
| α-helix | 61A-61B | 2 | |
| β-strand | 64-68 | 5 | 8 |
| β-strand | 72 | 1 | 9 |
| β-strand | 81-90 | 10 | 8 |
| β-strand | 104-108 | 5 | 8 |
| α-helix | 111-114 | 4 | |
| β-strand | 115 | 1 | 10 |
| β-strand | 120 | 1 | 10 |
| β-strand | 124A | 1 | 7 |
| α-helix | 129A-131 | 3 | |
| β-strand | 135-140 | 6 | 7 |
| α-helix | 150-152 | 3 | |
| β-strand | 154 | 1 | 9 |
| β-strand | 156-163 | 8 | 7 |
| α-helix | 164 | 1 | |
| α-helix | 165-169 | 5 | |
| β-strand | 180-183 | 4 | 7 |
| β-strand | 189 | 1 | 6 |
| β-strand | 198-201 | 4 | 7 |
| β-strand | 208-213 | 6 | 7 |
| β-strand | 226-230 | 5 | 7 |
| α-helix | 231-234 | 4 | |
| α-helix | 235-242 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Complement factor D | A, B | protein | 254 | Homo sapiens | P00746 (AlphaFold model) |
>6QMT_1 Complement factor D (chains A, B) HSWERLAVLVLLGAAACAAPPRGRILGGREAEAHARPYMASVQLNGAHLCGGVLVAEQWV LSAAHCLEDAADGKVQVLLGAHSLSQPEPSKRLYDVLRAVPHPDSQPDTIDHDLLLLQLS EKATLGPAVRPLPWQRVDRDVAPGTLCDVAGWGIVNHAGRRPDSLQHVLLPVLDRATCNR RTHHDGAITERLMCAESNRRDSCKGDSGGPLVCGGVLEGVVTSGSRVCGNRKKPGIYTRV ASYAAWIDSVLASA
| ID | Name | Formula | Copies |
|---|---|---|---|
| J7B | 2-[2-[[3-[3-(aminomethyl)phenyl]phenyl]carbonylamino]phenyl]ethanoic acid | C22 H20 N2 O3 | 2 |
Design, Synthesis, and Preclinical Characterization of Selective Factor D Inhibitors Targeting the Alternative Complement Pathway. Karki, R.G., Powers, J., Mainolfi, N. et al. J Med Chem (2019) 62:4656-4668. DOI 10.1021/acs.jmedchem.9b00271 · PubMed
Other PDB entries of the same protein (UniProt P00746 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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