Structure of PDB 5fbe Chain A

Receptor sequence
>5fbeA (length=228) Species: 9606 (Homo sapiens) [Search protein sequence]
ILGGREAEAHARPYMASVQLNGAHLCGGVLVAEQWVLSAAHCLEDAADGK
VQVLLGAHSLSQPEPSKRLYDVLRAVPHPDSQPDTIDHDLLLLQLSEKAT
LGPAVRPLPWQRVDRDVAPGTLCDVAGWGIVNHAGRRPDSLQHVLLPVLD
RATCNRRTHHDGAITERLMCAESNRRDSCKGDSGGPLVCGGVLEGVVTSG
SRVCGNRKKPGIYTRVASYAAWIDSVLA
3D structure
PDB5fbe Small-molecule factor D inhibitors targeting the alternative complement pathway.
ChainA
Resolution1.43 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H57 D102 K192 G193 D194 S195 G196
Catalytic site (residue number reindexed from 1) H41 D89 K180 G181 D182 S183 G184
Enzyme Commision number 3.4.21.46: complement factor D.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 5W5 A L41 C42 H57 C58 R151 S190 C191 K192 G193 S195 S215 R218 C220 L25 C26 H41 C42 R137 S178 C179 K180 G181 S183 S199 R202 C204 MOAD: ic50=14uM
PDBbind-CN: -logKd/Ki=4.85,IC50=14uM
BindingDB: IC50=14000nM
Gene Ontology
Molecular Function
GO:0004252 serine-type endopeptidase activity
GO:0008236 serine-type peptidase activity
Biological Process
GO:0006508 proteolysis
GO:0006956 complement activation
GO:0006957 complement activation, alternative pathway
GO:0009617 response to bacterium
Cellular Component
GO:0005576 extracellular region
GO:0005615 extracellular space
GO:0031093 platelet alpha granule lumen
GO:0034774 secretory granule lumen
GO:0070062 extracellular exosome
GO:1904813 ficolin-1-rich granule lumen

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5fbe, PDBe:5fbe, PDBj:5fbe
PDBsum5fbe
PubMed27775713
UniProtP00746|CFAD_HUMAN Complement factor D (Gene Name=CFD)

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