Structure of PDB 1rtk Chain A

Receptor sequence
>1rtkA (length=486) Species: 9606 (Homo sapiens) [Search protein sequence]
SMNIYLVLDGSDSIGASNFTGAKKVLVNLIEKVASYGVKPRYGLVTYATY
PKIWVKVSEADSSNADWVTKQLNEINYEDHKLKSGTNTKKALQAVYSMMS
WPGWNRTRHVIILMTDGLHNMGGDPITVIDEIRDLLYIGKDRKNPREDYL
DVYVFGVGPLVNQVNINALASKKDNEQHVCKVKDMECLEDVFYQMIDESQ
SLSLCGMVWEHRKGTDYHKQPWQAKISVIRKGHESCMGAVVSEYFVLTAA
HCFTVDDKEHSIKVSVGGEKRDLEIEVVLFHPNYNINGKKEAGIPEFYDY
DVALIKLKNKLKYGQTIRPICLPCTEGTTRALRLPPTTTCQQQKEELLPA
QDIKALFVSEEEKKLTRKEVYIKNGDKKGSCERDAQYAPGYDKVKDISEV
VTPRFLCTGGVSPYADPNTCRGDSGGPLIVHKRSRFIQVGVISWGVVDVC
KRQKQVPAHARDFHINLFQVLPWLKEKLQDEDLGFL
3D structure
PDB1rtk Structural analysis of engineered Bb fragment of complement factor B: insights into the activation mechanism of the alternative pathway C3-convertase.
ChainA
Resolution2.3 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) H251 D301 G422 S424 G425
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 A S253 S255 T328 S11 S13 T86
BS02 GBS A H501 R671 S674 S693 W694 G695 V697 D698 H251 R421 S424 S443 W444 G445 V447 D448
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:1rtk, PDBe:1rtk, PDBj:1rtk
PDBsum1rtk
PubMed15068800
UniProtP00751|CFAB_HUMAN Complement factor B (Gene Name=CFB)

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