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2APR

STRUCTURE AND REFINEMENT AT 1.8 ANGSTROMS RESOLUTION OF THE ASPARTIC PROTEINASE FROM RHIZOPUS CHINENSIS

Replaces:  1APR
Functional Information from GO Data
ChainGOidnamespacecontents
A0004190molecular_functionaspartic-type endopeptidase activity
A0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA A 326
ChainResidue
AGLY220
AHOH525
AHOH533
AHOH718
AHOH721
AHOH760
AHOH827

site_idCAT
Number of Residues2
DetailsCATALYTICALLY ACTIVE RESIDUES
ChainResidue
AASP35
AASP218

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. LDFDTGSSDLWI
ChainResidueDetails
ALEU32-ILE43
AGLY215-LEU226

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10094
ChainResidueDetails
AASP35
AASP218

218500

PDB entries from 2024-04-17

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