Structure of PDB 6fug Chain A

Receptor sequence
>6fugA (length=216) Species: 9606 (Homo sapiens) [Search protein sequence]
ILGGREAEAHARPYMASVQLNGAHLCGGVLVAEQWVLSAAHCLGKVQVLL
GAHSLSQPEPSKRLYDVLRAVPHPDSQPDTIDHDLLLLQLSEKATLGPAV
RPLPWQRVDRDVAPGTLCDVAGWGIVNHAGRRPDSLQHVLLPVLDRATCN
RAITERLMCAESNRRDSCKGDSGGPLVCGGVLEGVVTRVCGNRKKPGIYT
RVASYAAWIDSVLASA
3D structure
PDB6fug Discovery and Design of First Benzylamine-Based Ligands Binding to an Unlocked Conformation of the Complement Factor D.
ChainA
Resolution2.21 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 D84 K169 G170 D171 S172 G173
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 E85 A I143 H146 D189 S190 C191 K192 S195 V213 R218 V219 C220 I125 H128 D166 S167 C168 K169 S172 V186 R188 V189 C190 MOAD: Kd=50uM
PDBbind-CN: -logKd/Ki=4.30,Kd=50uM
BindingDB: IC50=20000nM,Kd=50000nM
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:6fug, PDBe:6fug, PDBj:6fug
PDBsum6fug
PubMed29795765
UniProtP00746|CFAD_HUMAN Complement factor D (Gene Name=CFD)

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