Structure of PDB 2xrc Chain C

Receptor sequence
>2xrcC (length=454) Species: 9606 (Homo sapiens) [Search protein sequence]
EDLVEKKCLAKKYTHLSCDKVFCQPWQRCIEGTCVCKLPYQCPKNGTAVC
ATNRRSFPTYCQQKSLECLHPGTKFLNNGTCTAEGKFSVSLKHGNTDSEG
IVEVKLVDQDKTMFICKSSWSMREANVACLDLGFQQGADTQRRFKLSDLS
CLHVHCRGLETSLAECTFTKRRTMGYQDFADVVCYTDFFQCVNGKYISQM
KACDGINDCGDQSDELCCKACQGKGFHCKSGVCIPSQYQCNGEVDCITGE
DEVGCAGMDAERRRIKSLLPKLSCGVPWQVAIKDAITCGGIYIGGCWILT
AAHCLTHRYQIWTTVRIVIEYVDRIIFHENYNAGTYQNDIALIEMKKDGN
KKDCELPRSIPACVPWSPYLFQPNDTCIVSGWLQWGEVKLISNCSKFYGN
RFYEKEMECAGTPLVCMDANNVTYVWGVVSWGENEFPGVYTKVANYFDWI
SYHV
3D structure
PDB2xrc Structural Basis for Complement Factor I Control and its Disease-Associated Sequence Polymorphisms.
ChainC
Resolution2.69 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H362 D411
Catalytic site (residue number reindexed from 1) H303 D339
Enzyme Commision number 3.4.21.45: complement factor I.
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 CA C Y258 N261 E263 D265 D271 E272 Y238 N241 E243 D245 D251 E252
BS02 CA C K221 D224 I226 D228 D234 E235 K201 D204 I206 D208 D214 E215
Gene Ontology
Molecular Function
GO:0004252 serine-type endopeptidase activity
GO:0005515 protein binding
GO:0008236 serine-type peptidase activity
GO:0046872 metal ion binding
Biological Process
GO:0006508 proteolysis
GO:0006956 complement activation
GO:0006958 complement activation, classical pathway
GO:0045087 innate immune response
Cellular Component
GO:0005576 extracellular region
GO:0005615 extracellular space
GO:0016020 membrane
GO:0070062 extracellular exosome

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2xrc, PDBe:2xrc, PDBj:2xrc
PDBsum2xrc
PubMed21768352
UniProtP05156|CFAI_HUMAN Complement factor I (Gene Name=CFI)

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