Complement factor D in complex with a reversible benzoic acid based inhibitor. Determined by X-ray diffraction at 1.65 Å resolution. Released 15 Feb 2017.
Explore 5MT4 in 3D Show helices and sheets RCSB PDB PDBe
5MT4 contains 7 α-helices and 20 β-strands across 1 chain. 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 | 57-59 | 3 | |
| β-strand | 64-68 | 5 | 3 |
| β-strand | 72 | 1 | 4 |
| β-strand | 81-90 | 10 | 3 |
| β-strand | 104-108 | 5 | 3 |
| β-strand | 115 | 1 | 5 |
| β-strand | 120 | 1 | 5 |
| α-helix | 122-124 | 3 | |
| β-strand | 124A | 1 | 2 |
| α-helix | 129A-131 | 3 | |
| β-strand | 135-140 | 6 | 2 |
| β-strand | 154 | 1 | 4 |
| β-strand | 156-163 | 8 | 2 |
| α-helix | 165-168 | 4 | |
| 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 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Complement factor D | A | protein | 232 | Homo sapiens | P00746 (AlphaFold model) |
>5MT4_1 Complement factor D (chains A) ILGGREAEAHARPYMASVQLNGAHLCGGVLVAEQWVLSAAHCLEDAADGKVQVLLGAHSL SQPEPSKRLYDVLRAVPHPDSQPDTIDHDLLLLQLSEKATLGPAVRPLPWQRVDRDVAPG TLCDVAGWGIVNHAGRRPDSLQHVLLPVLDRATCNRRTHHDGAITERLMCAESNRRDSCK GDSGGPLVCGGVLEGVVTSGSRVCGNRKKPGIYTRVASYAAWIDSVLASAAA
| ID | Name | Formula | Copies |
|---|---|---|---|
| M7O | 2-[(phenylmethyl)carbamoylamino]benzoic acid | C15 H14 N2 O3 | 1 |
Structure-Based Library Design and Fragment Screening for the Identification of Reversible Complement Factor D Protease Inhibitors. Vulpetti, A., Randl, S., Rudisser, S. et al. J Med Chem (2017) 60:1946-1958. DOI 10.1021/acs.jmedchem.6b01684 · 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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