6ULA

Crystal structure of human GAC in complex with inhibitor UPGL00012

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	13
Details	binding site for residue QA4 A 601

Chain	Residue
A	LYS320
B	ASN324
B	GLU325
B	TYR394
C	ARG317
A	LEU321
A	PHE322
A	LEU323
A	TYR394
B	LYS320
B	LEU321
B	PHE322
B	LEU323

---

site_id	AC2
Number of Residues	14
Details	binding site for residue QA4 C 601

Chain	Residue
C	PHE318
C	LYS320
C	LEU321
C	PHE322
C	LEU323
C	ASN324
C	TYR394
D	LYS320
D	LEU321
D	PHE322
D	LEU323
D	ASN324
D	GLU325
D	TYR394

---

site_id	AC3
Number of Residues	13
Details	binding site for residue QA4 E 602

Chain	Residue
E	LYS320
E	LEU321
E	PHE322
E	LEU323
E	GLU325
E	TYR394
G	LYS320
G	LEU321
G	PHE322
G	LEU323
G	ASN324
G	TYR394
H	ARG317

---

site_id	AC4
Number of Residues	17
Details	binding site for Di-peptide QA4 E 601 and ARG E 317

Chain	Residue
E	GLY315
E	LEU316
E	PHE318
F	LYS320
F	LEU321
F	PHE322
F	LEU323
F	TYR394
H	PHE318
H	LYS320
H	LEU321
H	PHE322
H	LEU323
H	ASN324
H	GLU325
H	ASP327
H	TYR394

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	48
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	TYR466
B	VAL484
C	SER286
C	ASN335
C	GLU381
C	TYR414
C	TYR466
C	VAL484
D	SER286
A	ASN335
D	ASN335
D	GLU381
D	TYR414
D	TYR466
D	VAL484
E	SER286
E	ASN335
E	GLU381
E	TYR414
E	TYR466
A	GLU381
E	VAL484
G	SER286
G	ASN335
G	GLU381
G	TYR414
G	TYR466
G	VAL484
F	SER286
F	ASN335
F	GLU381
A	TYR414
F	TYR414
F	TYR466
F	VAL484
H	SER286
H	ASN335
H	GLU381
H	TYR414
H	TYR466
H	VAL484
A	TYR466
A	VAL484
B	SER286
B	ASN335
B	GLU381

---

site_id	SWS_FT_FI2
Number of Residues	8
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
B	ASN388
C	ASN388
D	ASN388
E	ASN388
G	ASN388
F	ASN388
H	ASN388

---

site_id	SWS_FT_FI3
Number of Residues	8
Details	SITE: Cleavage; by MPP => ECO:0000250|UniProtKB:P13264

Chain	Residue	Details
A	LEU72
B	LEU72
C	LEU72
D	LEU72
E	LEU72
G	LEU72
F	LEU72
H	LEU72

---

site_id	SWS_FT_FI4
Number of Residues	16
Details	MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:D3Z7P3

Chain	Residue	Details
A	LYS130
E	LYS164
G	LYS130
G	LYS164
F	LYS130
F	LYS164
H	LYS130
H	LYS164
A	LYS164
B	LYS130
B	LYS164
C	LYS130
C	LYS164
D	LYS130
D	LYS164
E	LYS130

---

site_id	SWS_FT_FI5
Number of Residues	8
Details	MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861

Chain	Residue	Details
A	LYS311
B	LYS311
C	LYS311
D	LYS311
E	LYS311
G	LYS311
F	LYS311
H	LYS311

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