Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6NBK

Crystal structure of Arginase from Bacillus cereus

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000050	biological_process	urea cycle
A	0004053	molecular_function	arginase activity
A	0005737	cellular_component	cytoplasm
A	0006525	biological_process	arginine metabolic process
A	0016787	molecular_function	hydrolase activity
A	0016813	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
A	0030145	molecular_function	manganese ion binding
A	0046872	molecular_function	metal ion binding
B	0000050	biological_process	urea cycle
B	0004053	molecular_function	arginase activity
B	0005737	cellular_component	cytoplasm
B	0006525	biological_process	arginine metabolic process
B	0016787	molecular_function	hydrolase activity
B	0016813	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
B	0030145	molecular_function	manganese ion binding
B	0046872	molecular_function	metal ion binding
C	0000050	biological_process	urea cycle
C	0004053	molecular_function	arginase activity
C	0005737	cellular_component	cytoplasm
C	0006525	biological_process	arginine metabolic process
C	0016787	molecular_function	hydrolase activity
C	0016813	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
C	0030145	molecular_function	manganese ion binding
C	0046872	molecular_function	metal ion binding
D	0000050	biological_process	urea cycle
D	0004053	molecular_function	arginase activity
D	0005737	cellular_component	cytoplasm
D	0006525	biological_process	arginine metabolic process
D	0016787	molecular_function	hydrolase activity
D	0016813	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
D	0030145	molecular_function	manganese ion binding
D	0046872	molecular_function	metal ion binding
E	0000050	biological_process	urea cycle
E	0004053	molecular_function	arginase activity
E	0005737	cellular_component	cytoplasm
E	0006525	biological_process	arginine metabolic process
E	0016787	molecular_function	hydrolase activity
E	0016813	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
E	0030145	molecular_function	manganese ion binding
E	0046872	molecular_function	metal ion binding
F	0000050	biological_process	urea cycle
F	0004053	molecular_function	arginase activity
F	0005737	cellular_component	cytoplasm
F	0006525	biological_process	arginine metabolic process
F	0016787	molecular_function	hydrolase activity
F	0016813	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
F	0030145	molecular_function	manganese ion binding
F	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	binding site for residue MN A 301

Chain	Residue
A	ASP121
A	HIS123
A	ASP224
A	ASP226
A	MN302
A	HOH447
A	HOH556

site_id	AC2
Number of Residues	6
Details	binding site for residue MN A 302

Chain	Residue
A	ASP125
A	ASP224
A	MN301
A	HOH447
A	HIS98
A	ASP121

site_id	AC3
Number of Residues	7
Details	binding site for residue MN A 303

Chain	Residue
A	ASP82
A	GLU86
A	HOH483
F	GLU86
F	HOH461
F	HOH548
F	HOH551

site_id	AC4
Number of Residues	6
Details	binding site for residue CA A 304

Chain	Residue
A	ASP275
A	HOH448
A	HOH523
A	HOH648
D	ASP275
D	HOH503

site_id	AC5
Number of Residues	5
Details	binding site for residue MN B 301

Chain	Residue
B	HIS98
B	ASP121
B	ASP125
B	ASP224
B	MN302

site_id	AC6
Number of Residues	6
Details	binding site for residue MN B 302

Chain	Residue
B	ASP121
B	HIS123
B	ASP224
B	ASP226
B	MN301
B	HOH517

site_id	AC7
Number of Residues	6
Details	binding site for residue MN B 303

Chain	Residue
B	ASP82
B	GLU86
D	GLU86
D	HOH444
D	HOH501
D	HOH532

site_id	AC8
Number of Residues	6
Details	binding site for residue CA B 304

Chain	Residue
B	ASP275
B	HOH435
B	HOH493
F	ASP275
F	HOH487
F	HOH636

site_id	AC9
Number of Residues	6
Details	binding site for residue MN C 301

Chain	Residue
C	HIS98
C	ASP121
C	ASP125
C	ASP224
C	MN302
C	HOH444

site_id	AD1
Number of Residues	7
Details	binding site for residue MN C 302

Chain	Residue
C	ASP121
C	HIS123
C	ASP224
C	ASP226
C	MN301
C	HOH444
C	HOH525

site_id	AD2
Number of Residues	6
Details	binding site for residue CA C 303

Chain	Residue
C	ASP275
C	HOH447
E	ASP275
E	HOH437
E	HOH469
E	HOH599

site_id	AD3
Number of Residues	5
Details	binding site for residue MN D 301

Chain	Residue
D	HIS98
D	ASP121
D	ASP125
D	ASP224
D	MN302

site_id	AD4
Number of Residues	6
Details	binding site for residue MN D 302

Chain	Residue
D	ASP121
D	HIS123
D	ASP224
D	ASP226
D	MN301
D	HOH533

site_id	AD5
Number of Residues	7
Details	binding site for residue MN E 301

Chain	Residue
E	ASP121
E	HIS123
E	ASP224
E	ASP226
E	MN302
E	HOH452
E	HOH521

site_id	AD6
Number of Residues	6
Details	binding site for residue MN E 302

Chain	Residue
E	HIS98
E	ASP121
E	ASP125
E	ASP224
E	MN301
E	HOH452

site_id	AD7
Number of Residues	5
Details	binding site for residue MN F 301

Chain	Residue
F	HIS98
F	ASP121
F	ASP125
F	ASP224
F	MN302

site_id	AD8
Number of Residues	6
Details	binding site for residue MN F 302

Chain	Residue
F	ASP224
F	ASP226
F	MN301
F	HOH549
F	ASP121
F	HIS123

Functional Information from PROSITE/UniProt

site_id	PS01053
Number of Residues	22
Details	ARGINASE_1 Arginase family signature. SLDLDgldPhdaPGvgtpvigG

Chain	Residue	Details
A	SER222-GLY243

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)