Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3CEV

ARGINASE FROM BACILLUS CALDEVELOX, COMPLEXED WITH L-ARGININE

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	6
Details	BINDING SITE FOR RESIDUE MN A 300

Chain	Residue
A	HIS99
A	ASP122
A	ASP126
A	ASP226
A	ARG407
A	HOH408

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MN B 300

Chain	Residue
B	HIS99
B	ASP122
B	ASP126
B	ASP226
B	ARG408
B	HOH409

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MN C 300

Chain	Residue
C	HIS99
C	ASP122
C	ASP126
C	ASP226
C	ARG409
C	HOH410

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MN D 300

Chain	Residue
D	HIS99
D	ASP122
D	ASP126
D	ASP226
D	ARG410
D	HOH411

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MN E 300

Chain	Residue
E	HIS99
E	ASP122
E	ASP126
E	ASP226
E	ARG411
E	HOH412

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MN F 300

Chain	Residue
F	HIS99
F	ASP122
F	ASP126
F	ASP226
F	ARG412
F	HOH413

site_id	AC7
Number of Residues	11
Details	BINDING SITE FOR RESIDUE ARG A 401

Chain	Residue
A	HIS252
A	GLU256
A	SER292
A	GLU296
A	LEU298
A	HOH445
A	HOH499
B	MET195
B	HIS196
B	ASP199
B	HOH492

site_id	AC8
Number of Residues	11
Details	BINDING SITE FOR RESIDUE ARG B 402

Chain	Residue
B	HIS252
B	GLU256
B	SER292
B	GLU296
B	LEU298
B	HOH448
B	HOH505
C	MET195
C	HIS196
C	ASP199
C	HOH427

site_id	AC9
Number of Residues	11
Details	BINDING SITE FOR RESIDUE ARG C 403

Chain	Residue
A	MET195
A	HIS196
A	ASP199
A	HOH424
A	HOH489
C	HIS252
C	GLU256
C	SER292
C	GLU296
C	LEU298
C	HOH447

site_id	BC1
Number of Residues	10
Details	BINDING SITE FOR RESIDUE ARG D 404

Chain	Residue
D	HIS252
D	GLU256
D	SER292
D	GLU296
D	LEU298
D	HOH447
D	HOH500
E	HIS196
E	ASP199
E	HOH495

site_id	BC2
Number of Residues	11
Details	BINDING SITE FOR RESIDUE ARG E 405

Chain	Residue
E	HIS252
E	GLU256
E	SER292
E	GLU296
E	LEU298
E	HOH452
E	HOH507
F	MET195
F	HIS196
F	ASP199
F	HOH432

site_id	BC3
Number of Residues	11
Details	BINDING SITE FOR RESIDUE ARG F 406

Chain	Residue
D	MET195
D	HIS196
D	ASP199
D	HOH426
D	HOH489
F	HIS252
F	GLU256
F	SER292
F	GLU296
F	LEU298
F	HOH453

site_id	BC4
Number of Residues	18
Details	BINDING SITE FOR RESIDUE ARG A 407

Chain	Residue
A	HIS99
A	ASP126
A	ASN128
A	SER135
A	HIS139
A	ASP178
A	GLU181
A	ASP226
A	ASP228
A	THR240
A	GLU271
A	MN300
A	HOH408
A	HOH409
A	HOH410
A	HOH411
A	HOH455
A	HOH456

site_id	BC5
Number of Residues	19
Details	BINDING SITE FOR RESIDUE ARG B 408

Chain	Residue
B	HIS99
B	HIS124
B	ASP126
B	ASN128
B	SER135
B	HIS139
B	ASP178
B	GLU181
B	ASP226
B	ASP228
B	THR240
B	GLU271
B	MN300
B	HOH409
B	HOH414
B	HOH415
B	HOH416
B	HOH456
B	HOH457

site_id	BC6
Number of Residues	18
Details	BINDING SITE FOR RESIDUE ARG C 409

Chain	Residue
C	HIS99
C	ASP126
C	ASN128
C	SER135
C	HIS139
C	ASP178
C	GLU181
C	ASP226
C	ASP228
C	THR240
C	GLU271
C	MN300
C	HOH410
C	HOH414
C	HOH415
C	HOH416
C	HOH456
C	HOH457

site_id	BC7
Number of Residues	20
Details	BINDING SITE FOR RESIDUE ARG D 410

Chain	Residue
D	HIS99
D	HIS124
D	ASP126
D	ASN128
D	SER135
D	HIS139
D	ASP178
D	GLU181
D	ASP226
D	ASP228
D	THR240
D	GLU271
D	MN300
D	HOH411
D	HOH412
D	HOH413
D	HOH414
D	HOH434
D	HOH457
D	HOH458

site_id	BC8
Number of Residues	19
Details	BINDING SITE FOR RESIDUE ARG E 411

Chain	Residue
E	HIS99
E	HIS124
E	ASP126
E	ASN128
E	SER135
E	HIS139
E	ASP178
E	GLU181
E	ASP226
E	ASP228
E	THR240
E	GLU271
E	MN300
E	HOH412
E	HOH417
E	HOH418
E	HOH419
E	HOH439
E	HOH463

site_id	BC9
Number of Residues	19
Details	BINDING SITE FOR RESIDUE ARG F 412

Chain	Residue
F	HIS99
F	HIS124
F	ASP126
F	ASN128
F	SER135
F	HIS139
F	ASP178
F	GLU181
F	ASP226
F	ASP228
F	THR240
F	GLU271
F	MN300
F	HOH413
F	HOH419
F	HOH420
F	HOH421
F	HOH440
F	HOH462

site_id	MNA
Number of Residues	5
Details	SITE COMPRISES ONE MN ATOM, MN A 300, WHICH IS BOUND TO HIS 99 ND1, ASP 122 OD2, ASP 126 OD2, ASP 226 OD2, THE SUBSTRATE (R 7) NH2 AND WATER W1

Chain	Residue
A	MN300
A	HIS99
A	ASP122
A	ASP126
A	ASP226

site_id	MNB
Number of Residues	5
Details	SITE COMPRISES ONE MN ATOM, MN B 300, WHICH IS BOUND TO HIS 99 ND1, ASP 122 OD2, ASP 126 OD2, ASP 226 OD2, THE SUBSTRATE (R 8) NH2, AND A WATER W2

Chain	Residue
B	ASP226
B	MN300
B	HIS99
B	ASP122
B	ASP126

site_id	MNC
Number of Residues	5
Details	SITE COMPRISES ONE MN ATOM, MN C 300, WHICH IS BOUND TO HIS 99 ND1, ASP 122 OD2, ASP 126 OD2, ASP 226 OD2, THE SUBSTRATE (R 9) NH2 AND A WATER W3

Chain	Residue
C	MN300
C	HIS99
C	ASP122
C	ASP126
C	ASP226

site_id	MND
Number of Residues	5
Details	SITE COMPRISES ONE MN ATOM, MN D 300, WHICH IS BOUND TO HIS 99 ND1, ASP 122 OD2, ASP 126 OD2, ASP 226 OD2, THE SUBSTRATE (R 10) NH2 AND A WATER W4

Chain	Residue
D	MN300
D	HIS99
D	ASP122
D	ASP126
D	ASP226

site_id	MNE
Number of Residues	5
Details	SITE COMPRISES ONE MN ATOM, MN E 200, WHICH IS BOUND TO HIS 99 ND1, ASP 122 OD2, ASP 126 OD2, ASP 226 OD2, THE SUBSTRATE (R 11) NH2 AND A WATER W5

Chain	Residue
E	MN300
E	HIS99
E	ASP122
E	ASP126
E	ASP226

site_id	MNF
Number of Residues	5
Details	SITE COMPRISES ONE MN ATOM, MN F 200, WHICH IS BOUND TO HIS 99 ND1, ASP 122 OD2, ASP 126 OD2, ASP 226 OD2, THE SUBSTRATE (R 12) NH2 AND A WATER W6

Chain	Residue
F	MN300
F	HIS99
F	ASP122
F	ASP126
F	ASP226

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 site: {"evidences":[{"source":"PubMed","id":"10196128","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1CEV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2CEV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3CEV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4CEV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5CEV","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	24
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10196128","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1CEV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2CEV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4CEV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5CEV","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	42
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10196128","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3CEV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4CEV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5CEV","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10196128","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3CEV","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10196128","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3CEV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5CEV","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1cev

Chain	Residue	Details
A	ASP126
A	GLU271

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1cev

Chain	Residue	Details
B	ASP126
B	GLU271

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1cev

Chain	Residue	Details
C	ASP126
C	GLU271

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1cev

Chain	Residue	Details
D	ASP126
D	GLU271

site_id	CSA5
Number of Residues	2
Details	Annotated By Reference To The Literature 1cev

Chain	Residue	Details
E	ASP126
E	GLU271

site_id	CSA6
Number of Residues	2
Details	Annotated By Reference To The Literature 1cev

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)