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1MPP

X-RAY ANALYSES OF ASPARTIC PROTEINASES. V. STRUCTURE AND REFINEMENT AT 2.0 ANGSTROMS RESOLUTION OF THE ASPARTIC PROTEINASE FROM MUCOR PUSILLUS

Functional Information from GO Data
ChainGOidnamespacecontents
A0004190molecular_functionaspartic-type endopeptidase activity
A0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 501
ChainResidue
AARG86
ATYR133
AASN134
AASN139
AHOH562
AHOH564

site_idCAT
Number of Residues2
DetailsTHE ACTIVE SITE
ChainResidue
AASP32
AASP215

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. LLFDTGSSDTWV
ChainResidueDetails
ALEU29-VAL40
APHE212-ALA223

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE:
ChainResidueDetails
AASP32
AASP215

site_idSWS_FT_FI2
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine
ChainResidueDetails
AASN171

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PDB entries from 2024-07-17

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