6WZ4

Complex of mutant (K173M) of Pseudomonas 7A Glutaminase-Asparaginase with L-Asp at pH 6. Covalent acyl-enzyme intermediate

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004067	molecular_function	asparaginase activity
A	0004359	molecular_function	glutaminase activity
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	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	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	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	HOH612
A	HOH614
B	GLU294
B	HOH544
A	THR20
A	TYR34
A	ALA66
A	SER67
A	GLU68
A	GLY99
A	THR100
A	ASP101

---

site_id	AC2
Number of Residues	17
Details	binding site for Di-peptide ASP B 400 and THR B 20

Chain	Residue
A	GLU294
B	GLY19
B	ILE21
B	ALA22
B	GLY23
B	TYR34
B	ALA66
B	SER67
B	GLU68
B	GLY99
B	THR100
B	ASP101
B	SER125
B	ARG127
B	PRO128
B	HOH644
B	HOH646

---

site_id	AC3
Number of Residues	16
Details	binding site for Di-peptide ASP C 400 and THR C 20

Chain	Residue
C	GLY19
C	ILE21
C	ALA22
C	GLY23
C	TYR34
C	ALA66
C	SER67
C	GLU68
C	GLY99
C	THR100
C	ASP101
C	SER125
C	PRO128
C	HOH621
C	HOH624
D	GLU294

---

site_id	AC4
Number of Residues	18
Details	binding site for Di-peptide ASP D 400 and THR D 20

Chain	Residue
C	GLU294
C	HOH521
D	GLY19
D	ILE21
D	ALA22
D	GLY23
D	TYR34
D	ALA66
D	SER67
D	GLU68
D	GLY99
D	THR100
D	ASP101
D	SER125
D	ARG127
D	PRO128
D	HOH599
D	HOH642

---

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	1308
Details	Domain: {"description":"Asparaginase/glutaminase","evidences":[{"source":"PROSITE-ProRule","id":"PRU01068","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	Active site: {"description":"Acyl-ester intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU10099","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10100","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	8
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---