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3.4.21.110: C5a peptidase

This is an abbreviated version!
For detailed information about C5a peptidase, go to the full flat file.

Word Map on EC 3.4.21.110

Reaction

the primary cleavage site is at His67-/-Lys68 in human C5a with a minor secondary cleavage site at Ala58-/-Ser59 =

Synonyms

C5a peptidase, GBS, GBS C5a peptidase, S08.020, SCFI, SCPA, ScpB, scpI, SCPZ, SEZ C5a peptidase, streptococcal chemotactic factor inactivator, surface-bound C5a peptidase

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.110 C5a peptidase

Crystallization

Crystallization on EC 3.4.21.110 - C5a peptidase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
SCP mutant, by hanging drop method, to 2 A resolution, SCPB composed of five distinct domains, N-terminal subtilisin-like protease domain with a 134-residue protease-associated domain inserted into a loop between two beta-strands, and with one of two Arg-Gly-Asp sequences found in SCPB, at the C-terminus are three fibronectin type III domains, second Arg-Gly-Asp sequence is located between fibronectin type III (1) and fibronectin type III (2)
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crystal structure of an active form of ScpA is solved to 1.9 A resolution. The ScpA structure reveals that access to the catalytic site is restricted by variable regions in the catalytic domain and by the presence of the inserted protease-associated domain and the second fibronectin type III domains (Fn2). Modeling of the ScpA-C5a complex indicates that the substrate binds with carboxyl-terminal residues (65-74) extended through the active site and core residues (1-64) forming exosite-type interactions with the Fn2 domain. Substrate binding is anticipated to be dominated by ionic interactions in two distinct regions of ScpA. On the prime side of the active site, salt bridges are predicted between P1', P2', and P7' residues, and residues in the catalytic and PA domains. Remote to the active site, a larger number of ionic interactions between residues in the C5a core and the Fn2 domain are observed in the model. Thus, both PA and Fn2 domains are expected to play significant roles in substrate recognition
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