Structure of PDB 2odp Chain A

Receptor sequence

>2odpA (length=490) Species: 9606 (Homo sapiens)

KIQIQRSGHLNLYLLLDASQSVSENDFLIFKESASLMVDRIFSFEINVSV
AIITFASEPKVLMSVLNDNSRDMTEVISSLENANYKDHENGTGTNTYAAL
NSVYLMMNNQMRLLGMETMAWQEIRHAIILLTDGKSNMGGSPKTAVDHIR
EILNINQKRNDYLDIYAIGVGKLDVDWRELNELGSKKDGERHAFILQDTK
ALHQVFEHMLDVSKLTDTICGVGNMSANASDQERTPWHVTIKPTCRGALI
SDQWVLTAAHCFWRVNVGDPKSQWGKEFLIEKAVISPGFDVFAKKNQGIL
EFYGDDIALLKLAQKVKMSTHARPICLPCTMEANLALRRPQGSTCRDHEN
ELLNKQSVPAHFVALNGSKLNINLKMGVEWTSCAEVVSQEKTMFPNLTDV
REVVTDQFLCSGTQEDESPCKGESGGAVFLERRFRFFQVGLVSWGLYNPC
LNSRKRAPRSKVPPPRDFHINLFRMQPWLRQHLGDVLNFL

3D structure

• PDB: 2odp The crystal structure of c2a, the catalytic fragment of classical pathway c3 and c5 convertase of human complement.
• Chain: A
• Resolution: 1.9 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H487 D541 S659
• Catalytic site (residue number reindexed from 1): H260 D306 S424
• 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	MG	A	S242 S244 T317	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

External links

• PDB: RCSB:2odp, PDBe:2odp, PDBj:2odp
• PDBsum: 2odp
• PubMed: 17234210
• UniProt: Q5JP69