3LJQ

Crystal Structure of the Glycosylasparaginase T152C apo-precursor

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003948	molecular_function	N4-(beta-N-acetylglucosaminyl)-L-asparaginase activity
A	0005737	cellular_component	cytoplasm
A	0006508	biological_process	proteolysis
A	0008233	molecular_function	peptidase activity
A	0016787	molecular_function	hydrolase activity
A	0042597	cellular_component	periplasmic space
C	0003948	molecular_function	N4-(beta-N-acetylglucosaminyl)-L-asparaginase activity
C	0005737	cellular_component	cytoplasm
C	0006508	biological_process	proteolysis
C	0008233	molecular_function	peptidase activity
C	0016787	molecular_function	hydrolase activity
C	0042597	cellular_component	periplasmic space

Functional Information from PDB Data

site_id	AC1
Number of Residues	10
Details	BINDING SITE FOR RESIDUE GLY C 596

Chain	Residue
C	ASP451
C	HOH654
C	GLY472
C	MET473
C	ARG480
C	ASP483
C	SER484
C	GLY504
C	GLY506
C	HOH625

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site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NA A 597

Chain	Residue
A	VAL42
A	GLU43
A	ASP45
A	GLU48
A	VAL51
A	TYR53

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site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NA C 597

Chain	Residue
C	VAL342
C	ASP345
C	GLU348
C	VAL351
C	TYR353

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Nucleophile => ECO:0000269|PubMed:10490104, ECO:0000269|PubMed:17157318, ECO:0000269|PubMed:20800597, ECO:0000269|PubMed:9685368

Chain	Residue	Details
A	CYS152
C	CYS452

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site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING:

Chain	Residue	Details
A	ARG180
A	THR203
C	ARG480
C	THR503

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