6WYX

Crystal structure of Pseudomonas 7A Glutaminase-Asparaginase in complex with L-Asp at pH 5.0

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004067	molecular_function	asparaginase activity
A	0004359	molecular_function	glutaminase activity
A	0005829	cellular_component	cytosol
A	0006520	biological_process	amino acid metabolic process
A	0006528	biological_process	asparagine metabolic process
A	0016787	molecular_function	hydrolase activity
A	0042597	cellular_component	periplasmic space
A	0050417	molecular_function	glutamin-(asparagin-)ase activity
B	0004067	molecular_function	asparaginase activity
B	0004359	molecular_function	glutaminase activity
B	0005829	cellular_component	cytosol
B	0006520	biological_process	amino acid metabolic process
B	0006528	biological_process	asparagine metabolic process
B	0016787	molecular_function	hydrolase activity
B	0042597	cellular_component	periplasmic space
B	0050417	molecular_function	glutamin-(asparagin-)ase activity
C	0004067	molecular_function	asparaginase activity
C	0004359	molecular_function	glutaminase activity
C	0005829	cellular_component	cytosol
C	0006520	biological_process	amino acid metabolic process
C	0006528	biological_process	asparagine metabolic process
C	0016787	molecular_function	hydrolase activity
C	0042597	cellular_component	periplasmic space
C	0050417	molecular_function	glutamin-(asparagin-)ase activity
D	0004067	molecular_function	asparaginase activity
D	0004359	molecular_function	glutaminase activity
D	0005829	cellular_component	cytosol
D	0006520	biological_process	amino acid metabolic process
D	0006528	biological_process	asparagine metabolic process
D	0016787	molecular_function	hydrolase activity
D	0042597	cellular_component	periplasmic space
D	0050417	molecular_function	glutamin-(asparagin-)ase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	13
Details	binding site for residue ASP A 400

Chain	Residue
A	GLY19
A	HOH546
A	HOH618
B	GLU294
B	HOH520
A	THR20
A	ALA66
A	SER67
A	GLU68
A	GLY99
A	THR100
A	ASP101
A	SER125

---

site_id	AC2
Number of Residues	13
Details	binding site for residue ASP B 400

Chain	Residue
A	GLU294
A	HOH530
B	GLY19
B	THR20
B	ALA66
B	SER67
B	GLU68
B	GLY99
B	THR100
B	ASP101
B	SER125
B	HOH513
B	HOH680

---

site_id	AC3
Number of Residues	10
Details	binding site for residue GOL B 401

Chain	Residue
B	ALA83
B	GLU87
B	VAL113
B	GLU114
B	LYS115
B	ASP214
B	ILE215
B	HOH562
B	HOH575
B	HOH692

---

site_id	AC4
Number of Residues	14
Details	binding site for residue ASP C 400

Chain	Residue
C	GLY19
C	THR20
C	ALA66
C	SER67
C	GLU68
C	GLY99
C	THR100
C	ASP101
C	SER125
C	HOH596
C	HOH676
C	HOH709
D	GLU294
D	HOH532

---

site_id	AC5
Number of Residues	15
Details	binding site for residue ASP D 400

Chain	Residue
C	GLU294
C	HOH531
D	GLY19
D	THR20
D	ALA66
D	SER67
D	GLU68
D	GLY99
D	THR100
D	ASP101
D	SER125
D	HOH518
D	HOH520
D	HOH667
D	HOH728

---

Functional Information from PROSITE/UniProt

site_id	PS00144
Number of Residues	9
Details	ASN_GLN_ASE_1 Asparaginase / glutaminase active site signature 1. IlATGGTIA

Chain	Residue	Details
A	ILE14-ALA22

---

site_id	PS00917
Number of Residues	11
Details	ASN_GLN_ASE_2 Asparaginase / glutaminase active site signature 2. GiVitHGTDTL

Chain	Residue	Details
A	GLY93-LEU103

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Acyl-ester intermediate => ECO:0000255|PROSITE-ProRule:PRU10099, ECO:0000255|PROSITE-ProRule:PRU10100

Chain	Residue	Details
B	THR20
C	THR20
D	THR20
A	THR20

---

site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
C	SER67
C	THR100
D	SER67
D	THR100
A	THR100
B	SER67
B	THR100
A	SER67

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