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1E81

Endothiapepsin complex with renin inhibitor MERCK-KGAA-EMD61395

Functional Information from GO Data
ChainGOidnamespacecontents
E0004190molecular_functionaspartic-type endopeptidase activity
E0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE M91 E 400
ChainResidue
EASP12
EGLY217
ETHR218
ETHR219
EPHE284
EHOH2013
EHOH2147
EASP30
EASP32
ETYR75
EGLY76
EASP77
EASP114
EPHE189
EASP215

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. LDFDTGSSDLWV
ChainResidueDetails
ELEU29-VAL40
EGLY212-LEU223

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE:
ChainResidueDetails
EASP32
ESER194

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
EASP32

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
EASP215

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
EASP215
ESER35
ETHR218
EASP32

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
EASP215
ETHR216
EASP32
ETHR33

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
EASP215
ESER35
EASP32

site_idCSA6
Number of Residues4
DetailsAnnotated By Reference To The Literature 1am5
ChainResidueDetails
EASP215
ETHR218
EASP32
ETHR33

222415

PDB entries from 2024-07-10

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