Structure of PDB 6fuh Chain A

Receptor sequence
>6fuhA (length=228) Species: 9606 (Homo sapiens) [Search protein sequence]
ILGGREAEAHARPYMASVQLNGAHLCGGVLVAEQWVLSAAHCLEDAADGK
VQVLLGAHSLSQPEPSKRLYDVLRAVPHPDSQPDTIDHDLLLLQLSEKAT
LGPAVRPLPWQRVDRDVAPGTLCDVAGWGIVNHAGRRPDSLQHVLLPVLD
RATCNRRTHHDGAITERLMCAESNRRDSCKGDSGGPLVCGGVLEGVVTSG
SRVCGNRKKPGIYTRVASYAAWIDSVLA
3D structure
PDB6fuh Discovery and Design of First Benzylamine-Based Ligands Binding to an Unlocked Conformation of the Complement Factor D.
ChainA
Resolution1.37 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 E88 A C42 H57 D189 S190 C191 K192 G193 S195 V213 S215 S217 R218 C26 H41 D177 S178 C179 K180 G181 S183 V197 S199 S201 R202 MOAD: Kd=170uM
PDBbind-CN: -logKd/Ki=3.77,Kd=170uM
BindingDB: Kd=170000nM,IC50=75000nM
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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Biological Process
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Cellular Component
External links
PDB RCSB:6fuh, PDBe:6fuh, PDBj:6fuh
PDBsum6fuh
PubMed29795765
UniProtP00746|CFAD_HUMAN Complement factor D (Gene Name=CFD)

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