1LYW

CATHEPSIN D AT PH 7.5

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004190	molecular_function	aspartic-type endopeptidase activity
A	0006508	biological_process	proteolysis
B	0004190	molecular_function	aspartic-type endopeptidase activity
B	0006508	biological_process	proteolysis
C	0004190	molecular_function	aspartic-type endopeptidase activity
C	0006508	biological_process	proteolysis
D	0004190	molecular_function	aspartic-type endopeptidase activity
D	0006508	biological_process	proteolysis
E	0004190	molecular_function	aspartic-type endopeptidase activity
E	0006508	biological_process	proteolysis
F	0004190	molecular_function	aspartic-type endopeptidase activity
F	0006508	biological_process	proteolysis
G	0004190	molecular_function	aspartic-type endopeptidase activity
G	0006508	biological_process	proteolysis
H	0004190	molecular_function	aspartic-type endopeptidase activity
H	0006508	biological_process	proteolysis

Functional Information from PDB Data

site_id	AC1
Number of Residues	12
Details	BINDING SITE FOR RESIDUE EPE A 98

Chain	Residue
A	ASN38
B	GLY116
B	VAL144
B	VAL147
A	LEU39
A	TRP40
A	PHE74
A	TYR78
A	LEU83
A	LEU87
B	VAL114
B	PHE115

---

site_id	AC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE EPE C 98

Chain	Residue
C	TYR10
C	SER36
C	ASN38
C	LEU39
C	TRP40
C	TYR78
D	PHE115
D	GLY116
D	ILE134
D	VAL144

---

site_id	AC3
Number of Residues	13
Details	BINDING SITE FOR RESIDUE EPE G 98

Chain	Residue
G	ASN38
G	LEU39
G	TRP40
G	PHE74
G	ILE76
G	TYR78
G	LEU83
G	LEU87
G	HOH115
G	HOH128
H	VAL114
H	PHE115
H	VAL144

---

site_id	AC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE EPE E 98

Chain	Residue
E	TYR10
E	ASN38
E	LEU39
E	TRP40
E	LEU83
E	HOH130
F	ILE134
F	VAL144

---

Functional Information from PROSITE/UniProt

site_id	PS00141
Number of Residues	12
Details	ASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. AIVDTGTSLMVG

Chain	Residue	Details
B	ALA228-GLY239
A	VAL30-VAL41

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10094","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"8393577","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"12754519","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16263699","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8393577","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1lya

Chain	Residue	Details
A	ASP33
B	ASP231

---

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1lya

Chain	Residue	Details
C	ASP33
D	ASP231

---

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1lya

Chain	Residue	Details
F	ASP231
E	ASP33

---

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1lya

Chain	Residue	Details
H	ASP231
G	ASP33

---