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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 Residues304
DetailsDomain: {"description":"Peptidase A1","evidences":[{"source":"PROSITE-ProRule","id":"PRU01103","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10094","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
Detailsa catalytic site defined by CSA, PubMed 3316666, 895839, 3036594, 11714911
ChainResidueDetails
ATHR221
ASER38
AASP35
AASP218

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PDB entries from 2025-11-05

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