8SZJ

Human glutaminase C (Y466W) with L-Gln and Pi, filamentous form

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004359	molecular_function	glutaminase activity
A	0006541	biological_process	glutamine metabolic process
B	0004359	molecular_function	glutaminase activity
B	0006541	biological_process	glutamine metabolic process
C	0004359	molecular_function	glutaminase activity
C	0006541	biological_process	glutamine metabolic process
D	0004359	molecular_function	glutaminase activity
D	0006541	biological_process	glutamine metabolic process
E	0004359	molecular_function	glutaminase activity
E	0006541	biological_process	glutamine metabolic process
F	0004359	molecular_function	glutaminase activity
F	0006541	biological_process	glutamine metabolic process
G	0004359	molecular_function	glutaminase activity
G	0006541	biological_process	glutamine metabolic process
H	0004359	molecular_function	glutaminase activity
H	0006541	biological_process	glutamine metabolic process
I	0004359	molecular_function	glutaminase activity
I	0006541	biological_process	glutamine metabolic process
J	0004359	molecular_function	glutaminase activity
J	0006541	biological_process	glutamine metabolic process
K	0004359	molecular_function	glutaminase activity
K	0006541	biological_process	glutamine metabolic process
L	0004359	molecular_function	glutaminase activity
L	0006541	biological_process	glutamine metabolic process

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	72
Details	BINDING: BINDING => ECO:0000269|PubMed:22049910, ECO:0000269|PubMed:22538822, ECO:0000305|PubMed:24451979, ECO:0007744|PDB:3CZD, ECO:0007744|PDB:3UNW, ECO:0007744|PDB:3VP0, ECO:0007744|PDB:3VP1

Chain	Residue	Details
A	SER286
B	TYR414
B	TRP466
B	VAL484
C	SER286
C	ASN335
C	GLU381
C	TYR414
C	TRP466
C	VAL484
D	SER286
A	ASN335
D	ASN335
D	GLU381
D	TYR414
D	TRP466
D	VAL484
E	SER286
E	ASN335
E	GLU381
E	TYR414
E	TRP466
A	GLU381
E	VAL484
G	SER286
G	ASN335
G	GLU381
G	TYR414
G	TRP466
G	VAL484
I	SER286
I	ASN335
I	GLU381
A	TYR414
I	TYR414
I	TRP466
I	VAL484
K	SER286
K	ASN335
K	GLU381
K	TYR414
K	TRP466
K	VAL484
F	SER286
A	TRP466
F	ASN335
F	GLU381
F	TYR414
F	TRP466
F	VAL484
H	SER286
H	ASN335
H	GLU381
H	TYR414
H	TRP466
A	VAL484
H	VAL484
J	SER286
J	ASN335
J	GLU381
J	TYR414
J	TRP466
J	VAL484
L	SER286
L	ASN335
L	GLU381
B	SER286
L	TYR414
L	TRP466
L	VAL484
B	ASN335
B	GLU381

---

site_id	SWS_FT_FI2
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269|PubMed:22049910, ECO:0000269|PubMed:22538822, ECO:0000305|PubMed:24451979, ECO:0007744|PDB:3CZD, ECO:0007744|PDB:3UNW, ECO:0007744|PDB:3VP1

Chain	Residue	Details
A	ASN388
H	ASN388
J	ASN388
L	ASN388
B	ASN388
C	ASN388
D	ASN388
E	ASN388
G	ASN388
I	ASN388
K	ASN388
F	ASN388

---

site_id	SWS_FT_FI3
Number of Residues	12
Details	SITE: Cleavage; by MPP => ECO:0000250|UniProtKB:P13264

Chain	Residue	Details
A	LEU72
H	LEU72
J	LEU72
L	LEU72
B	LEU72
C	LEU72
D	LEU72
E	LEU72
G	LEU72
I	LEU72
K	LEU72
F	LEU72

---

site_id	SWS_FT_FI4
Number of Residues	24
Details	MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:D3Z7P3

Chain	Residue	Details
A	LYS130
E	LYS164
G	LYS130
G	LYS164
I	LYS130
I	LYS164
K	LYS130
K	LYS164
F	LYS130
F	LYS164
H	LYS130
A	LYS164
H	LYS164
J	LYS130
J	LYS164
L	LYS130
L	LYS164
B	LYS130
B	LYS164
C	LYS130
C	LYS164
D	LYS130
D	LYS164
E	LYS130

---

site_id	SWS_FT_FI5
Number of Residues	12
Details	MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861

Chain	Residue	Details
A	LYS311
H	LYS311
J	LYS311
L	LYS311
B	LYS311
C	LYS311
D	LYS311
E	LYS311
G	LYS311
I	LYS311
K	LYS311
F	LYS311

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