4GID

Structure of beta-secretase complexed with inhibitor

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004190	molecular_function	aspartic-type endopeptidase activity
A	0006508	biological_process	proteolysis
A	0016020	cellular_component	membrane
B	0004190	molecular_function	aspartic-type endopeptidase activity
B	0006508	biological_process	proteolysis
B	0016020	cellular_component	membrane
C	0004190	molecular_function	aspartic-type endopeptidase activity
C	0006508	biological_process	proteolysis
C	0016020	cellular_component	membrane
D	0004190	molecular_function	aspartic-type endopeptidase activity
D	0006508	biological_process	proteolysis
D	0016020	cellular_component	membrane

Functional Information from PDB Data

site_id	AC1
Number of Residues	24
Details	BINDING SITE FOR RESIDUE 0GH A 501

Chain	Residue
A	GLY59
A	GLN121
A	PHE156
A	ILE166
A	TYR246
A	ASP276
A	SER277
A	GLY278
A	THR279
A	THR280
A	ASN281
A	GLN60
A	ARG283
A	SER373
A	ALA383
A	HOH692
A	HOH875
A	GLY61
A	LEU78
A	ASP80
A	GLY82
A	PRO118
A	TYR119
A	THR120

---

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE LPD A 502

Chain	Residue
A	GLY56
A	CYS203
A	GLY204
A	ALA205
A	LEU209
A	SER217
A	VAL218

---

site_id	AC3
Number of Residues	24
Details	BINDING SITE FOR RESIDUE 0GH B 501

Chain	Residue
B	GLY59
B	GLN60
B	GLY61
B	LEU78
B	ASP80
B	GLY82
B	SER83
B	TYR119
B	THR120
B	GLN121
B	PHE156
B	ILE158
B	ILE166
B	TYR246
B	ASP276
B	SER277
B	GLY278
B	THR279
B	THR280
B	ASN281
B	ARG283
B	SER373
B	ALA383
B	HOH879

---

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE LPD B 502

Chain	Residue
B	GLY56
B	CYS203
B	ALA205
B	LEU209
B	SER217
B	VAL218

---

site_id	AC5
Number of Residues	24
Details	BINDING SITE FOR RESIDUE 0GH C 501

Chain	Residue
C	GLY59
C	GLN60
C	GLY61
C	ASP80
C	GLY82
C	PRO118
C	TYR119
C	THR120
C	GLN121
C	PHE156
C	ILE158
C	ILE174
C	TYR246
C	ASP276
C	SER277
C	GLY278
C	THR279
C	THR280
C	ASN281
C	ARG283
C	SER373
C	ALA383
C	HOH701
C	HOH836

---

site_id	AC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE LPD C 502

Chain	Residue
C	GLY56
C	CYS203
C	ALA205
C	LEU209
C	SER217
C	VAL218
C	GLY219

---

site_id	AC7
Number of Residues	24
Details	BINDING SITE FOR RESIDUE 0GH D 501

Chain	Residue
D	THR120
D	GLN121
D	PHE156
D	ILE158
D	ILE166
D	TYR246
D	ASP276
D	SER277
D	GLY278
D	THR279
D	THR280
D	ASN281
D	ARG283
D	SER373
D	ALA383
D	HOH713
D	HOH889
D	GLY59
D	GLN60
D	GLY61
D	ASP80
D	GLY82
D	PRO118
D	TYR119

---

site_id	AC8
Number of Residues	8
Details	BINDING SITE FOR RESIDUE LPD D 502

Chain	Residue
D	GLY56
D	CYS203
D	ALA205
D	LEU209
D	SER217
D	VAL218
D	GLY219
D	HOH736

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ILE77-VAL88

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	ACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10094

Chain	Residue	Details
A	ASP80
A	ASP276
B	ASP80
B	ASP276
C	ASP80
C	ASP276
D	ASP80
D	ASP276

---

site_id	SWS_FT_FI2
Number of Residues	28
Details	MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:17425515, ECO:0000269|PubMed:19011241

Chain	Residue	Details
A	LYS113
A	LYS262
A	LYS266
A	LYS272
A	LYS286
A	LYS287
A	LYS294
B	LYS113
B	LYS262
B	LYS266
B	LYS272
B	LYS286
B	LYS287
B	LYS294
C	LYS113
C	LYS262
C	LYS266
C	LYS272
C	LYS286
C	LYS287
C	LYS294
D	LYS113
D	LYS262
D	LYS266
D	LYS272
D	LYS286
D	LYS287
D	LYS294

---

site_id	SWS_FT_FI3
Number of Residues	16
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255

Chain	Residue	Details
A	ASN140
A	ASN159
A	ASN210
A	ASN341
B	ASN140
B	ASN159
B	ASN210
B	ASN341
C	ASN140
C	ASN159
C	ASN210
C	ASN341
D	ASN140
D	ASN159
D	ASN210
D	ASN341

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