Structure of PDB 2i6q Chain A

Receptor sequence
>2i6qA (length=503) Species: 9606 (Homo sapiens) [Search protein sequence]
SKIQIQRSGHLNLYLLLDCSQSVSENDFLIFKESASLMVDRIFSFEINVS
VAIITFASEPKVLMSVLNDNSRDMTEVISSLENANYKDHENGTGTNTYAA
LNSVYLMMNNQMRLLGMETMAWQEIRHAIILLTDGKSNMGGSPKTAVDHI
REILNINQKRNDYLDIYAIGVGKLDVDWRELNELGSKKDGERHAFILQDT
KALHQVFEHMLDVSKLTDTICGVGNMSANASDQERTPWHVTIKPKSQETC
RGALISDQWVLTAAHCFRDGNDHSLWRVNVGDPKSQWGKEFLIEKAVISP
GFDVFAKKNQGILEFYGDDIALLKLAQKVKMSTHARPICLPCTMEANLAL
RRPQGSTCRDHENELLNKQSVPAHFVALNGSKLNINLKMGVEWTSCAEVV
SQEKTMFPNLTDVREVVTDQFLCSGTQEDESPCKGESGGAVFLERRFRFF
QVGLVSWGLYNPCLRKRAPRSKVPPPRDFHINLFRMQPWLRQHLGDVLNF
LPL
3D structure
PDB2i6q Structure of complement component c2a: implications for convertase formation and substrate binding.
ChainA
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) H487 D541
Catalytic site (residue number reindexed from 1) H265 D319
Enzyme Commision number 3.4.21.43: classical-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 MN A S242 S244 T317 S20 S22 T95
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:2i6q, PDBe:2i6q, PDBj:2i6q
PDBsum2i6q
PubMed17027507
UniProtP06681|CO2_HUMAN Complement C2 (Gene Name=C2)

[Back to BioLiP]