1as4

CLEAVED ANTICHYMOTRYPSIN A349RCLEAVED ANTICHYMOTRYPSIN A349R

Structural highlights

1as4 is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.1Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

AACT_HUMAN Although its physiological function is unclear, it can inhibit neutrophil cathepsin G and mast cell chymase, both of which can convert angiotensin-1 to the active angiotensin-2.^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

↑ Rubin H, Wang ZM, Nickbarg EB, McLarney S, Naidoo N, Schoenberger OL, Johnson JL, Cooperman BS. Cloning, expression, purification, and biological activity of recombinant native and variant human alpha 1-antichymotrypsins. J Biol Chem. 1990 Jan 15;265(2):1199-207. PMID:2404007

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OCA

[1] Rubin H, Wang ZM, Nickbarg EB, McLarney S, Naidoo N, Schoenberger OL, Johnson JL, Cooperman BS. Cloning, expression, purification, and biological activity of recombinant native and variant human alpha 1-antichymotrypsins. J Biol Chem. 1990 Jan 15;265(2):1199-207. PMID:2404007

[1]

1as4

CLEAVED ANTICHYMOTRYPSIN A349RCLEAVED ANTICHYMOTRYPSIN A349R

Structural highlights

Function

Evolutionary Conservation

See Also

References

Contents

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1as4

CLEAVED ANTICHYMOTRYPSIN A349RCLEAVED ANTICHYMOTRYPSIN A349R

Structural highlights

Function

Evolutionary Conservation

See Also

References

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