Structure of PDB 5nb6 Chain A

Receptor sequence
>5nb6A (length=216) Species: 9606 (Homo sapiens) [Search protein sequence]
ILGGREAEAHARPYMASVQLNGAHLCGGVLVAEQWVLSAAHCLEGKVQVL
LGAHSLSQPEPSKRLYDVLRAVPHPDSQPDTIDHDLLLLQLSEKATLGPA
VRPLPWQRVDRDVAPGTLCDVAGWGIVNHAGRRPDSLQHVLLPVLDRATC
NERLMCAESNRRDSCKGDSGGPLVCGGVLEGVVTSGSRVCGNRKKPGIYT
RVASYAAWIDSVLASA
3D structure
PDB5nb6 Discovery of Highly Potent and Selective Small-Molecule Reversible Factor D Inhibitors Demonstrating Alternative Complement Pathway Inhibition in Vivo.
ChainA
Resolution1.75 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 K166 G167 D168 S169 G170
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 8S2 A H40 L41 C42 R151 C191 K192 G193 S195 T214 S215 G216 R218 H24 L25 C26 R133 C165 K166 G167 S169 T184 S185 G186 R188 MOAD: ic50=0.5uM
PDBbind-CN: -logKd/Ki=6.30,IC50=0.50uM
BindingDB: IC50=667nM
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:5nb6, PDBe:5nb6, PDBj:5nb6
PDBsum5nb6
PubMed28621538
UniProtP00746|CFAD_HUMAN Complement factor D (Gene Name=CFD)

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