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1RNE

THE CRYSTAL STRUCTURE OF RECOMBINANT GLYCOSYLATED HUMAN RENIN ALONE AND IN COMPLEX WITH A TRANSITION STATE ANALOG INHIBITOR

Functional Information from GO Data
ChainGOidnamespacecontents
A0004190molecular_functionaspartic-type endopeptidase activity
A0006508biological_processproteolysis
Functional Information from PDB Data
site_idCAT
Number of Residues2
DetailsCATALYTIC ASPARTIC ACID RESIDUES
ChainResidue
AASP32
AASP215

site_idS1
Number of Residues9
DetailsSUBSTRATE BINDING SUBSITE 1
ChainResidue
AVAL30
AASP32
ATYR75
ATHR77
APHE112
APHE117
AVAL120
AASP215
AGLY217

site_idS1'
Number of Residues7
DetailsSUBSTRATE BINDING SUBSITE 1'
ChainResidue
ASER76
ALEU213
AASP215
AILE291
APRO292
ATHR295
AALA300

site_idS2
Number of Residues8
DetailsSUBSTRATE BINDING SUBSITE 2
ChainResidue
ASER76
ATHR77
AALA218
ASER222
AHIS287
AMET289
AILE291
AALA300

site_idS2'
Number of Residues7
DetailsSUBSTRATE BINDING SUBSITE 2'
ChainResidue
AGLY34
ASER35
ALEU73
AARG74
ATYR75
AGLN128
AILE130

site_idS3
Number of Residues9
DetailsSUBSTRATE BINDING SUBSITE 3
ChainResidue
ATHR77
APRO111
APHE112
ALEU114
AALA115
APHE117
ASER219
ATHR12
AGLN13

site_idS4
Number of Residues5
DetailsSUBSTRATE BINDING SUBSITE 4
ChainResidue
ATHR12
ASER219
ATYR220
APHE242
AHIS287

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. VVFDTGSSNVWV
ChainResidueDetails
AVAL29-VAL40
AALA212-GLY223

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:20927107
ChainResidueDetails
AASP32
AASP215

site_idSWS_FT_FI2
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:2493678
ChainResidueDetails
AASN-1
AASN67

Catalytic Information from CSA
site_idCSA1
Number of Residues3
Detailsa catalytic site defined by CSA, PubMed 1807356, 11714911
ChainResidueDetails
AASP215
ASER35
AASP32

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PDB entries from 2024-09-04

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