Structure of PDB 5tcc Chain E

Receptor sequence
>5tccE (length=228) Species: 9606 (Homo sapiens) [Search protein sequence]
ILGGREAEAHARPYMASVQLNGAHLCGGVLVAEQWVLSAAHCLEDAADGK
VQVLLGAHSLSQPEPSKRLYDVLRAVPHPDSQPDTIDHDLLLLQLSEKAT
LGPAVRPLPWQRVDRDVAPGTLCDVAGWGIVNHAGRRPDSLQHVLLPVLD
RATCNRRTHHDGAITERLMCAESNRRDSCKGDSGGPLVCGGVLEGVVTSG
SRVCGNRKKPGIYTRVASYAAWIDSVLA
3D structure
PDB5tcc Buried Hydrogen Bond Interactions Contribute to the High Potency of Complement Factor D Inhibitors.
ChainE
Resolution3.37 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) 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 E 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
BS02 J56 E G18 L137 L160 P162 G3 L122 L145 P147 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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5tcc, PDBe:5tcc, PDBj:5tcc
PDBsum5tcc
PubMed27994744
UniProtP00746|CFAD_HUMAN Complement factor D (Gene Name=CFD)

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