Structure of PDB 6rur Chain J

Receptor sequence
>6rurJ (length=505) Species: 9606 (Homo sapiens) [Search protein sequence]
KIVLDPSGSMNIYLVLDGSGSIGASNFTGAKKCLVNLIEKVASYGVKPRY
GLVTYATYPKIWVKVSEADSSNADWVTKQLNEINYEDHKLKSGTNTKKAL
QAVYSMMSWPDDVPPEGWNRTRHVIILMTDGLHNMGGDPITVIDEIRDLL
YIGKDRKNPREDYLDVYVFGVGPLVNQVNINALASKKDNEQHVFKVKDME
NLEDVFYQMIDESQSLSLCGMVWEHRKGTDYHKQPWQAKISVIRPSKGHE
SCMGAVVSEYFVLTAAHCFTVDDKEHSIKVSVGGEKRDLEIEVVLFHPNY
NINGKKEAGIPEFYDYDVALIKLKNKLKYGQTIRPICLPCTEGTTRALRL
PPTTTCQQQKEELLPAQDIKALFVSEEEKKLTRKEVYIKNGDKKGSCERD
AQYAPGYDKVKDISEVVTPRFLCTGGVSPYADPNTCRGDAGGPLIVHKRS
RFIQVGVISWGVVDVCKNQKRQKQVPAHARDFHINLFQVLPWLKEKLQDE
DLGFL
3D structure
PDB6rur Structural Basis for Properdin Oligomerization and Convertase Stimulation in the Human Complement System.
ChainJ
Resolution6.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H501 D551 G672 A674 G675
Catalytic site (residue number reindexed from 1) H267 D317 G438 A440 G441
Enzyme Commision number 3.4.21.47: alternative-complement-pathway C3/C5 convertase.
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 MG J S253 S255 T328 D364 S19 S21 T94 D130
Gene Ontology
Molecular Function
GO:0004252 serine-type endopeptidase activity
Biological Process
GO:0006508 proteolysis
GO:0006956 complement activation
Cellular Component
GO:0005576 extracellular region

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:6rur, PDBe:6rur, PDBj:6rur
PDBsum6rur
PubMed31507604
UniProtP00751|CFAB_HUMAN Complement factor B (Gene Name=CFB)

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