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

1ZAP

SECRETED ASPARTIC PROTEASE FROM C. ALBICANS

Functional Information from GO Data
ChainGOidnamespacecontents
A0004190molecular_functionaspartic-type endopeptidase activity
A0005576cellular_componentextracellular region
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN A 400
ChainResidue
AASP57
AGLU324
AHOH672

site_idAC2
Number of Residues20
DetailsBINDING SITE FOR RESIDUE A70 A 500
ChainResidue
AGLY34
ATYR84
AGLY85
AASP86
AILE119
AILE123
AASN131
AGLU193
AASP218
AGLY220
ATHR221
ATHR222
AASN301
AILE305
AHOH632
AHOH902
AVAL12
ATHR13
AILE30
AASP32

site_idACT
Number of Residues2
DetailsASPARTIC PROTEINASES ARE CHARACTERIZED BY TWO ASP RESIDUES, ONE FROM EACH DOMAIN, CORRESPONDING TO PEPSIN ASP 32, ASP 218.
ChainResidue
AASP32
AASP218

Functional Information from PROSITE/UniProt
site_idPS00141
Number of Residues12
DetailsASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. VIVDTGSSDLWV
ChainResidueDetails
AVAL29-VAL40
AVAL215-LEU226

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10094
ChainResidueDetails
AASP32
AASP218

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P0CY29
ChainResidueDetails
AASP32
AGLY85
AASP191
AASP214
AASP218

site_idSWS_FT_FI3
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN257
AASN265

218853

PDB entries from 2024-04-24

PDB statisticsPDBj update infoContact PDBjnumon