9C97

Yeast 20S proteasome soaked with BRA-346 fraction

Functional Information from GO Data

Chain	GOid	namespace	contents
N	0000502	cellular_component	proteasome complex
N	0004175	molecular_function	endopeptidase activity
N	0004298	molecular_function	threonine-type endopeptidase activity
N	0005515	molecular_function	protein binding
N	0005634	cellular_component	nucleus
N	0005737	cellular_component	cytoplasm
N	0005829	cellular_component	cytosol
N	0006508	biological_process	proteolysis
N	0008233	molecular_function	peptidase activity
N	0010499	biological_process	proteasomal ubiquitin-independent protein catabolic process
N	0016787	molecular_function	hydrolase activity
N	0019774	cellular_component	proteasome core complex, beta-subunit complex
N	0034515	cellular_component	proteasome storage granule
N	0043161	biological_process	proteasome-mediated ubiquitin-dependent protein catabolic process
b	0000502	cellular_component	proteasome complex
b	0004175	molecular_function	endopeptidase activity
b	0004298	molecular_function	threonine-type endopeptidase activity
b	0005515	molecular_function	protein binding
b	0005634	cellular_component	nucleus
b	0005737	cellular_component	cytoplasm
b	0005829	cellular_component	cytosol
b	0006508	biological_process	proteolysis
b	0008233	molecular_function	peptidase activity
b	0010499	biological_process	proteasomal ubiquitin-independent protein catabolic process
b	0016787	molecular_function	hydrolase activity
b	0019774	cellular_component	proteasome core complex, beta-subunit complex
b	0034515	cellular_component	proteasome storage granule
b	0043161	biological_process	proteasome-mediated ubiquitin-dependent protein catabolic process

Functional Information from PROSITE/UniProt

site_id	PS00388
Number of Residues	23
Details	PROTEASOME_ALPHA_1 Proteasome alpha-type subunits signature. YdrgvStFSPeGRlfQVEYSleA

Chain	Residue	Details
D	TYR0-ALA22
G	TYR3-ALA25
F	TYR4-ALA26
C	TYR2-ALA24
A	TYR5-ALA27
B	TYR5-SER27
E	TYR5-ALA27

---

site_id	PS00854
Number of Residues	47
Details	PROTEASOME_BETA_1 Proteasome beta-type subunits signature. VAMtGkdCVAIACDlrlgsqslgvsnkfe.Kifhyghvflgit.GlaTD

Chain	Residue	Details
I	VAL12-ASP58
K	LEU4-ASP51
H	VAL4-ASP51
b	MET4-ASP51
J	LEU5-ASP52
L	LEU13-ASP60
C	VAL32-ASP79
B	ILE35-ASP82
a	ILE12-ASP59

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	24
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"22106047","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"17287358","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"17330950","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17330950","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17330950","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17330950","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	6
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	6
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"9087403","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI9
Number of Residues	2
Details	Modified residue: {"description":"N-acetylmethionine","evidences":[{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI10
Number of Residues	2
Details	Binding site: {}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	8
Details	M-CSA 177

Chain	Residue	Details
O	MET1	covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor
O	LYS17	activator, steric locator
O	GLY19	activator
O	THR33	activator, electrostatic stabiliser
O	THR47	electrostatic stabiliser
O	PRO129	activator, electrostatic stabiliser
O	LYS166	activator, steric locator
O	VAL169	activator, electrostatic stabiliser

---

site_id	MCSA2
Number of Residues	8
Details	M-CSA 177

Chain	Residue	Details
V	THR1	covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor
V	ASP17	activator, steric locator
V	ARG19	activator
V	LYS33	activator, electrostatic stabiliser
V	GLY47	electrostatic stabiliser
V	SER129	activator, electrostatic stabiliser
V	ASP166	activator, steric locator
V	SER169	activator, electrostatic stabiliser

---