Structure of PDB 2win Chain J

Receptor sequence
>2winJ (length=507) Species: 9606 (Homo sapiens) [Search protein sequence]
KIVLDPSGSMNIYLVLDGSDSIGASNFTGAKKCLVNLIEKVASYGVKPRY
GLVTYATYPKIWVKVSEADSSNADWVTKQLNEINYEDHKLKSGTNTKKAL
QAVYSMMSWPDDVPPEGWNRTRHVIILMTDGLHNMGGDPITVIDEIRDLL
YIGKDRKNPREDYLDVYVFGVGPLVNQVNINALASKKDNEQHVFKVKDME
NLEDVFYQMIDESQSLSLCGMVWEHRKGTDYHKQPWQAKISVIRPSKGHE
SCMGAVVSEYFVLTAAHCFTVDDKEHSIKVSVGGEKRDLEIEVVLFHPNY
NINGKKEAGIPEFYDYDVALIKLKNKLKYGQTIRPICLPCTEGTTRALRL
PPTTTCQQQKEELLPAQDIKALFVSEEEKKLTRKEVYIKNGDKKGSCERD
AQYAPGYDKVKDISEVVTPRFLCTGGVSPYADPNTCRGDSGGPLIVHKRS
RFIQVGVISWGVVDVCKNQKRQKQVPAHARDFHINLFQVLPWLKEKLQDE
DLGFLAA
3D structure
PDB2win Structural and functional implications of the alternative complement pathway C3 convertase stabilized by a staphylococcal inhibitor.
ChainJ
Resolution3.9 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 S674 G675
Catalytic site (residue number reindexed from 1) H267 D317 G438 S440 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 S19 S21 T94
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:2win, PDBe:2win, PDBj:2win
PDBsum2win
PubMed19503103
UniProtP00751|CFAB_HUMAN Complement factor B (Gene Name=CFB)

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