Structure of PDB 5tcc Chain C

Receptor sequence

>5tccC (length=228) Species: 9606 (Homo sapiens)

ILGGREAEAHARPYMASVQLNGAHLCGGVLVAEQWVLSAAHCLEDAADGK
VQVLLGAHSLSQPEPSKRLYDVLRAVPHPDSQPDTIDHDLLLLQLSEKAT
LGPAVRPLPWQRVDRDVAPGTLCDVAGWGIVNHAGRRPDSLQHVLLPVLD
RATCNRRTHHDGAITERLMCAESNRRDSCKGDSGGPLVCGGVLEGVVTSG
SRVCGNRKKPGIYTRVASYAAWIDSVLA

3D structure

• PDB: 5tcc Buried Hydrogen Bond Interactions Contribute to the High Potency of Complement Factor D Inhibitors.
• Chain: C
• Resolution: 3.37 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H56 D104 K195 G196 D197 S198 G199
• 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	J56	C	H148 A149	H133 A134	BindingDB: IC50=77nM,Kd=2210nM
BS02	J56	C	L40 C41 H56 C57 K195 G196 S198 S214 G215 S216 R217	L25 C26 H41 C42 K180 G181 S183 S199 G200 S201 R202	BindingDB: IC50=77nM,Kd=2210nM
BS03	J56	C	L137 H158 L160 P162 R191	L122 H143 L145 P147 R176	BindingDB: IC50=77nM,Kd=2210nM

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

External links

• PDB: RCSB:5tcc, PDBe:5tcc, PDBj:5tcc
• PDBsum: 5tcc
• PubMed: 27994744
• UniProt: P00746|CFAD_HUMAN Complement factor D (Gene Name=CFD)