Brand  (β version)

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Ligands
Code Name Link
ACT Acetate ion
Code : 1AS4
Header : SERPIN
Title : CLEAVED ANTICHYMOTRYPSIN A349R
Release Data : 1998-02-25
Compound :
mol_id molecule chains synonym
1 ANTICHYMOTRYPSIN A ACT
fragment: CHAIN A CONTAINS RESIDUES 20 - 358, CHAIN B CONTAINS RESIDUES 359 - 393
mutation: A349R
other_details: CLEAVED ANTICHYMOTRYPSIN
mol_id molecule chains synonym
2 ANTICHYMOTRYPSIN B ACT
fragment: CHAIN A CONTAINS RESIDUES 20 - 358, CHAIN B CONTAINS RESIDUES 359 - 393
mutation: A349R
other_details: CLEAVED ANTICHYMOTRYPSIN
Source :
mol_id organism_scientific organism_common expression_system
1 Homo sapiens  (taxid:9606) Human Escherichia coli  (taxid:562)
gene: ACT
expression_system_plasmid: PZMS
expression_system_gene: ACT
mol_id organism_scientific organism_common expression_system
2 Homo sapiens  (taxid:9606) Human Escherichia coli  (taxid:562)
gene: ACT
expression_system_plasmid: PZMS
expression_system_gene: ACT
Authors : Lukacs, C.M., Christianson, D.W.
Keywords : SERPIN, SERINE PROTEASE INHIBITOR, ANTICHYMOTRYPSIN
Exp. method : X-RAY DIFFRACTION ( 2.1 Å )
Citation :

Engineering an anion-binding cavity in antichymotrypsin modulates the "spring-loaded" serpin-protease interaction.

Lukacs, C.M.,Rubin, H.,Christianson, D.W.
(1998)  Biochemistry  37 : 3297 - 3304

PubMed: 9521649
DOI: 10.1021/bi972359e

Arginine Substitutions in the Hinge Region of Antichymotrypsin Affect Serpin Beta-Sheet Rearrangement

Lukacs, C.M.,Zhong, J.Q.,Plotnick, M.I.  et al.
(1996)  Nat.Struct.Biol.  3 : 888

Chain : B
UniProt : P01011 (AACT_HUMAN)
Reaction : -