Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

4AMT

Crystal structure at 2.6A of human prorenin

Functional Information from GO Data
ChainGOidnamespacecontents
A0001822biological_processkidney development
A0001823biological_processmesonephros development
A0002003biological_processangiotensin maturation
A0002016biological_processregulation of blood volume by renin-angiotensin
A0002018biological_processrenin-angiotensin regulation of aldosterone production
A0004175molecular_functionendopeptidase activity
A0004190molecular_functionaspartic-type endopeptidase activity
A0005102molecular_functionsignaling receptor binding
A0005159molecular_functioninsulin-like growth factor receptor binding
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005886cellular_componentplasma membrane
A0006508biological_processproteolysis
A0008217biological_processregulation of blood pressure
A0008233molecular_functionpeptidase activity
A0008584biological_processmale gonad development
A0009410biological_processresponse to xenobiotic stimulus
A0009755biological_processhormone-mediated signaling pathway
A0010033biological_processobsolete response to organic substance
A0016020cellular_componentmembrane
A0032496biological_processresponse to lipopolysaccharide
A0035902biological_processresponse to immobilization stress
A0042756biological_processdrinking behavior
A0043408biological_processregulation of MAPK cascade
A0045177cellular_componentapical part of cell
A0048469biological_processcell maturation
A0050435biological_processamyloid-beta metabolic process
A0051591biological_processresponse to cAMP
A0070305biological_processresponse to cGMP
A0071466biological_processcellular response to xenobiotic stimulus
A0072051biological_processjuxtaglomerular apparatus development
Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. VVFDTGSSNVWV
ChainResidueDetails
AVAL78-VAL89
AALA266-GLY277

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:20927107
ChainResidueDetails
AASP81
AASP269

site_idSWS_FT_FI2
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:2493678
ChainResidueDetails
AASN48
AASN118

222624

PDB entries from 2024-07-17

PDB statisticsPDBj update infoContact PDBjnumon