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Search The CSA
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Catalytic Site Atlas

CSA LITERATURE entry for 2apr

E.C. namerhizopuspepsin
SpeciesRhizopus chinensis (Bread mold)
E.C. Number (IntEnz) 3.4.23.21
CSA Homologues of 2aprThere are 272 Homologs
CSA Entries With UniProtID P06026
CSA Entries With EC Number 3.4.23.21
PDBe Entry 2apr
PDBSum Entry 2apr
MACiE Entry 2apr

Literature Report

Introduction
Mechansim
Reaction

Catalytic Sites for 2apr

Annotated By Reference To The Literature - Site 3 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
ThrA221289macie:sideChain
SerA38106macie:sideChain
AspA35103macie:sideChain
AspA218286macie:sideChain

Literature References

Notes:
Suguna K
Structure and refinement at 1.8 A resolution of the aspartic proteinase from Rhizopus chinensis.
J Mol Biol 1987 196 877-900
PubMed: 3316666
James MN
Mechanism of acid protease catalysis based on the crystal structure of penicillopepsin.
Nature 1977 267 808-813
PubMed: 895839
Polgár L.
The mechanism of action of aspartic proteases involves 'push-pull' catalysis.
FEBS Lett 1987 219 1-4
PubMed: 3036594
Andreeva NS
Analysis of crystal structures of aspartic proteinases: on the role of amino acid residues adjacent to the catalytic site of pepsin-like enzymes.
Protein Sci 2001 10 2439-2450
PubMed: 11714911
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