Structure of PDB 1rrk Chain A

Receptor sequence
>1rrkA (length=480) Species: 9606 (Homo sapiens) [Search protein sequence]
SMNIYLVLDGSDSIGASNFTGAKKVLVNLIEKVASYGVKPRYGLVTYATY
PKIWVKVSEADSSNADWVTKQLNEINYEDHKLKSGTNTKKALQAVYSMMS
WPGWNRTRHVIILMTDGLHNMGGDPITVIDEIRDLLYIGKDRNPREDYLD
VYVFGVGPLVNQVNINALASKKDNEQHVCKVKDMECLEDVFYQMIDESQS
LSLCGMVWEHRKGTDYHKQPWQAKISVIRKGHESCMGAVVSEYFVLTAAH
CFTVDDKEHSIKVSVGGEKRDLEIEVVLFHPNYNINGKKEAGIPEFYDYD
VALIKLKNKLKYGQTIRPICLPCTEGTTRALRLPPTTTCQQQKEELLPAQ
DIKALFVSEEEKKLTRKEVYIKNGDKKGSCERDAQYAPGYDKVKDISEVV
TPRFLCTGGVSPYADPNTCRGDSGGPLIVHKRSRFIQVGVISWGVVDVCV
PAHARDFHINLFQVLPWLKEKLQDEDLGFL
3D structure
PDB1rrk Structural analysis of engineered Bb fragment of complement factor B: insights into the activation mechanism of the alternative pathway C3-convertase.
ChainA
Resolution2.0 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 S674 G675
Catalytic site (residue number reindexed from 1) H250 D300 G421 S423 G424
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 CO A S253 S255 T328 S11 S13 T86
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:1rrk, PDBe:1rrk, PDBj:1rrk
PDBsum1rrk
PubMed15068800
UniProtP00751|CFAB_HUMAN Complement factor B (Gene Name=CFB)

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