Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1CEV

ARGINASE FROM BACILLUS CALDOVELOX, NATIVE STRUCTURE AT PH 5.6

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	0019547	biological_process	arginine catabolic process to ornithine
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	0019547	biological_process	arginine catabolic process to ornithine
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	0019547	biological_process	arginine catabolic process to ornithine
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	0019547	biological_process	arginine catabolic process to ornithine
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	0019547	biological_process	arginine catabolic process to ornithine
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	0019547	biological_process	arginine catabolic process to ornithine
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	5
Details	BINDING SITE FOR RESIDUE MN A 300

Chain	Residue
A	HIS99
A	ASP122
A	ASP126
A	ASP226
A	MN301

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN A 301

Chain	Residue
A	ASP122
A	HIS124
A	ASP226
A	ASP228
A	MN300

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN B 300

Chain	Residue
B	HIS99
B	ASP122
B	ASP126
B	ASP226

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN B 301

Chain	Residue
B	ASP122
B	HIS124
B	ASP226
B	ASP228

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN C 300

Chain	Residue
C	HIS99
C	ASP122
C	ASP126
C	ASP226
C	MN301

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN C 301

Chain	Residue
C	ASP122
C	HIS124
C	ASP226
C	ASP228
C	MN300

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN D 300

Chain	Residue
D	HIS99
D	ASP122
D	ASP126
D	ASP226
D	MN301

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN D 301

Chain	Residue
D	ASP122
D	HIS124
D	ASP226
D	ASP228
D	MN300

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN E 300

Chain	Residue
E	HIS99
E	ASP122
E	ASP126
E	ASP226

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN E 301

Chain	Residue
E	ASP122
E	HIS124
E	ASP226
E	ASP228

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN F 300

Chain	Residue
F	HIS99
F	ASP122
F	ASP126
F	ASP226
F	MN301

site_id	BC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN F 301

Chain	Residue
F	ASP122
F	HIS124
F	ASP226
F	ASP228
F	MN300

site_id	MNA
Number of Residues	8
Details	SITE COMPRISES TWO MN ATOMS, MN A 300 AND MN A 301 MN A 300 BOUND TO HIS 99 ND1, ASP 122 OD2, ASP 126 OD2 AND ASP 226 OD2. MN A 301 BOUND TO HIS 124 ND1, ASP 122 OD1, ASP 226 OD2, ASP 228 OD1, AND ASP 228 OD2.

Chain	Residue
A	MN300
A	MN301
A	HIS99
A	ASP122
A	HIS124
A	ASP126
A	ASP226
A	ASP228

site_id	MNB
Number of Residues	8
Details	SITE COMPRISES TWO MN ATOMS, MN B 300 AND MN B 301 MN B 300 BOUND TO HIS 99 ND1, ASP 122 OD2, ASP 126 OD2, AND ASP 226 OD2. MN B 301 BOUND TO HIS 124 ND1, ASP 122 OD1, ASP 226 OD2, ASP 228 OD1, AND ASP 228 OD2.

Chain	Residue
B	MN301
B	HIS99
B	ASP122
B	HIS124
B	ASP126
B	ASP226
B	ASP228
B	MN300

site_id	MNC
Number of Residues	8
Details	SITE COMPRISES TWO MN ATOMS, MN C 300 AND MN C 301 MN C 300 BOUND TO HIS 99 ND1, ASP 122 OD2, ASP 126 OD2, AND ASP 226 OD2. MN C 301 BOUND TO HIS 124 ND1, ASP 122 OD1, ASP 226 OD2, ASP 228 OD1, AND ASP 228 OD2.

Chain	Residue
C	MN300
C	MN301
C	HIS99
C	ASP122
C	HIS124
C	ASP126
C	ASP226
C	ASP228

site_id	MND
Number of Residues	8
Details	SITE COMPRISES TWO MN ATOMS, MN D 300 AND MN D 301 MN D 300 BOUND TO HIS 99 ND1, ASP 122 OD2, ASP 126 OD2, AND ASP 226 OD2. MN D 301 BOUND TO HIS 124 ND1, ASP 122 OD1, ASP 226 OD2, ASP 228 OD1, AND ASP 228 OD2.

Chain	Residue
D	MN300
D	MN301
D	HIS99
D	ASP122
D	HIS124
D	ASP126
D	ASP226
D	ASP228

site_id	MNE
Number of Residues	8
Details	SITE COMPRISES TWO MN ATOMS, MN E 300 AND MN E 301 MN E 300 BOUND TO HIS 99 ND1, ASP 122 OD2, ASP 126 OD2, AND ASP 226 OD2. MN E 301 BOUND TO HIS 124 ND1, ASP 122 OD1, ASP 226 OD2, ASP 228 OD1, AND ASP 228 OD2.

Chain	Residue
E	MN300
E	MN301
E	HIS99
E	ASP122
E	HIS124
E	ASP126
E	ASP226
E	ASP228

site_id	MNF
Number of Residues	8
Details	SITE COMPRISES TWO MN ATOMS, MN F 300 AND MN F 301 MN F 300 BOUND TO HIS 99 ND1, ASP 122 OD2, ASP 126 OD2, AND ASP 226 OD2. MN F 301 BOUND TO HIS 124 ND1, ASP 122 OD1, ASP 226 OD2, ASP 228 OD1, AND ASP 228 OD2.

Chain	Residue
F	MN300
F	MN301
F	HIS99
F	ASP122
F	HIS124
F	ASP126
F	ASP226
F	ASP228

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	SER224-GLY245

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269\|PubMed:10196128, ECO:0007744\|PDB:1CEV, ECO:0007744\|PDB:2CEV, ECO:0007744\|PDB:3CEV, ECO:0007744\|PDB:4CEV, ECO:0007744\|PDB:5CEV

Chain	Residue	Details
A	HIS99
E	ASP126
F	HIS99
F	ASP126
A	ASP126
B	HIS99
B	ASP126
C	HIS99
C	ASP126
D	HIS99
D	ASP126
E	HIS99

site_id	SWS_FT_FI2
Number of Residues	24
Details	BINDING: BINDING => ECO:0000269\|PubMed:10196128, ECO:0007744\|PDB:1CEV, ECO:0007744\|PDB:2CEV, ECO:0007744\|PDB:4CEV, ECO:0007744\|PDB:5CEV

Chain	Residue	Details
A	ASP122
C	HIS124
C	ASP226
C	ASP228
D	ASP122
D	HIS124
D	ASP226
D	ASP228
E	ASP122
E	HIS124
E	ASP226
A	HIS124
E	ASP228
F	ASP122
F	HIS124
F	ASP226
F	ASP228
A	ASP226
A	ASP228
B	ASP122
B	HIS124
B	ASP226
B	ASP228
C	ASP122

site_id	SWS_FT_FI3
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269\|PubMed:10196128, ECO:0007744\|PDB:3CEV, ECO:0007744\|PDB:4CEV, ECO:0007744\|PDB:5CEV

Chain	Residue	Details
A	SER135
E	ASP178
F	SER135
F	ASP178
A	ASP178
B	SER135
B	ASP178
C	SER135
C	ASP178
D	SER135
D	ASP178
E	SER135

site_id	SWS_FT_FI4
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269\|PubMed:10196128, ECO:0007744\|PDB:3CEV

Chain	Residue	Details
A	THR240
B	THR240
C	THR240
D	THR240
E	THR240
F	THR240

site_id	SWS_FT_FI5
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269\|PubMed:10196128, ECO:0007744\|PDB:3CEV, ECO:0007744\|PDB:5CEV

Chain	Residue	Details
A	GLU271
B	GLU271
C	GLU271
D	GLU271
E	GLU271
F	GLU271

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	a catalytic site defined by CSA, PubMed 10542097, 11258879, 11258880

Chain	Residue	Details
A	ASP126
A	GLU271

site_id	CSA2
Number of Residues	2
Details	a catalytic site defined by CSA, PubMed 10542097, 11258879, 11258880

Chain	Residue	Details
B	ASP126
B	GLU271

site_id	CSA3
Number of Residues	2
Details	a catalytic site defined by CSA, PubMed 10542097, 11258879, 11258880

Chain	Residue	Details
C	ASP126
C	GLU271

site_id	CSA4
Number of Residues	2
Details	a catalytic site defined by CSA, PubMed 10542097, 11258879, 11258880

Chain	Residue	Details
D	ASP126
D	GLU271

site_id	CSA5
Number of Residues	2
Details	a catalytic site defined by CSA, PubMed 10542097, 11258879, 11258880

Chain	Residue	Details
E	ASP126
E	GLU271

site_id	CSA6
Number of Residues	2
Details	a catalytic site defined by CSA, PubMed 10542097, 11258879, 11258880

Chain	Residue	Details
F	ASP126
F	GLU271

site_id	MCSA1
Number of Residues	8
Details	M-CSA 445

Chain	Residue	Details
A	HIS99	metal ligand
A	ASP122	metal ligand
A	HIS124	metal ligand
A	ASP126	metal ligand, modifies pKa, proton shuttle (general acid/base)
A	HIS139	proton shuttle (general acid/base), steric role
A	ASP226	metal ligand
A	ASP228	metal ligand
A	GLU271	electrostatic stabiliser, steric role

site_id	MCSA2
Number of Residues	8
Details	M-CSA 445

Chain	Residue	Details
B	HIS99	metal ligand
B	ASP122	metal ligand
B	HIS124	metal ligand
B	ASP126	metal ligand, modifies pKa, proton shuttle (general acid/base)
B	HIS139	proton shuttle (general acid/base), steric role
B	ASP226	metal ligand
B	ASP228	metal ligand
B	GLU271	electrostatic stabiliser, steric role

site_id	MCSA3
Number of Residues	8
Details	M-CSA 445

Chain	Residue	Details
C	HIS99	metal ligand
C	ASP122	metal ligand
C	HIS124	metal ligand
C	ASP126	metal ligand, modifies pKa, proton shuttle (general acid/base)
C	HIS139	proton shuttle (general acid/base), steric role
C	ASP226	metal ligand
C	ASP228	metal ligand
C	GLU271	electrostatic stabiliser, steric role

site_id	MCSA4
Number of Residues	8
Details	M-CSA 445

Chain	Residue	Details
D	HIS99	metal ligand
D	ASP122	metal ligand
D	HIS124	metal ligand
D	ASP126	metal ligand, modifies pKa, proton shuttle (general acid/base)
D	HIS139	proton shuttle (general acid/base), steric role
D	ASP226	metal ligand
D	ASP228	metal ligand
D	GLU271	electrostatic stabiliser, steric role

site_id	MCSA5
Number of Residues	8
Details	M-CSA 445

Chain	Residue	Details
E	HIS99	metal ligand
E	ASP122	metal ligand
E	HIS124	metal ligand
E	ASP126	metal ligand, modifies pKa, proton shuttle (general acid/base)
E	HIS139	proton shuttle (general acid/base), steric role
E	ASP226	metal ligand
E	ASP228	metal ligand
E	GLU271	electrostatic stabiliser, steric role

site_id	MCSA6
Number of Residues	8
Details	M-CSA 445

Chain	Residue	Details
F	HIS99	metal ligand
F	ASP122	metal ligand
F	HIS124	metal ligand
F	ASP126	metal ligand, modifies pKa, proton shuttle (general acid/base)
F	HIS139	proton shuttle (general acid/base), steric role
F	ASP226	metal ligand
F	ASP228	metal ligand
F	GLU271	electrostatic stabiliser, steric role

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)