Structure of PDB 5fck Chain A

Receptor sequence
>5fckA (length=225) Species: 9606 (Homo sapiens) [Search protein sequence]
ILGGREAEAHARPYMASVQLNGAHLCGGVLVAEQWVLSAAHCLDGKVQVL
LGAHSLSQPEPSKRLYDVLRAVPHPDSQPDTIDHDLLLLQLSEKATLGPA
VRPLPWQRVDRDVAPGTLCDVAGWGIVNHAGRRPDSLQHVLLPVLDRATC
NRRTHHDGAITERLMCAESNRRDSCKGDSGGPLVCGGVLEGVVTSGSRVC
GNRKKPGIYTRVASYAAWIDSVLAS
3D structure
PDB5fck Small-molecule factor D inhibitors targeting the alternative complement pathway.
ChainA
Resolution1.86 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 D85 K176 G177 D178 S179 G180
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 5WC A H40 L41 C42 H57 C58 R151 C191 K192 G193 S195 S215 G216 S217 R218 C220 H24 L25 C26 H41 C42 R133 C175 K176 G177 S179 S195 G196 S197 R198 C200 MOAD: Kd=0.006uM
PDBbind-CN: -logKd/Ki=8.22,Kd=0.006uM
BindingDB: IC50=10nM
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:5fck, PDBe:5fck, PDBj:5fck
PDBsum5fck
PubMed27775713
UniProtP00746|CFAD_HUMAN Complement factor D (Gene Name=CFD)

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