4RLA

ALTERING THE BINUCLEAR MANGANESE CLUSTER OF ARGINASE DIMINISHES THERMOSTABILITY AND CATALYTIC FUNCTION

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000050	biological_process	urea cycle
A	0001889	biological_process	liver development
A	0001938	biological_process	positive regulation of endothelial cell proliferation
A	0002250	biological_process	adaptive immune response
A	0004053	molecular_function	arginase activity
A	0005615	cellular_component	extracellular space
A	0005737	cellular_component	cytoplasm
A	0005741	cellular_component	mitochondrial outer membrane
A	0005829	cellular_component	cytosol
A	0006525	biological_process	arginine metabolic process
A	0007565	biological_process	female pregnancy
A	0009410	biological_process	response to xenobiotic stimulus
A	0009635	biological_process	response to herbicide
A	0010042	biological_process	response to manganese ion
A	0010043	biological_process	response to zinc ion
A	0010269	biological_process	response to selenium ion
A	0014075	biological_process	response to amine
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	0030324	biological_process	lung development
A	0032496	biological_process	response to lipopolysaccharide
A	0032964	biological_process	collagen biosynthetic process
A	0033189	biological_process	response to vitamin A
A	0033197	biological_process	response to vitamin E
A	0042130	biological_process	negative regulation of T cell proliferation
A	0042802	molecular_function	identical protein binding
A	0042832	biological_process	defense response to protozoan
A	0043025	cellular_component	neuronal cell body
A	0043200	biological_process	response to amino acid
A	0043434	biological_process	response to peptide hormone
A	0045087	biological_process	innate immune response
A	0046007	biological_process	negative regulation of activated T cell proliferation
A	0046686	biological_process	response to cadmium ion
A	0046872	molecular_function	metal ion binding
A	0048545	biological_process	response to steroid hormone
A	0048678	biological_process	response to axon injury
A	0051597	biological_process	response to methylmercury
A	0060056	biological_process	mammary gland involution
A	0060135	biological_process	maternal process involved in female pregnancy
A	0060336	biological_process	negative regulation of type II interferon-mediated signaling pathway
A	0070301	biological_process	cellular response to hydrogen peroxide
A	0070965	biological_process	positive regulation of neutrophil mediated killing of fungus
A	0071222	biological_process	cellular response to lipopolysaccharide
A	0071353	biological_process	cellular response to interleukin-4
A	0071377	biological_process	cellular response to glucagon stimulus
A	0071549	biological_process	cellular response to dexamethasone stimulus
A	0071560	biological_process	cellular response to transforming growth factor beta stimulus
A	1905541	biological_process	regulation of L-arginine import across plasma membrane
A	2000552	biological_process	negative regulation of T-helper 2 cell cytokine production
B	0000050	biological_process	urea cycle
B	0001889	biological_process	liver development
B	0001938	biological_process	positive regulation of endothelial cell proliferation
B	0002250	biological_process	adaptive immune response
B	0004053	molecular_function	arginase activity
B	0005615	cellular_component	extracellular space
B	0005737	cellular_component	cytoplasm
B	0005741	cellular_component	mitochondrial outer membrane
B	0005829	cellular_component	cytosol
B	0006525	biological_process	arginine metabolic process
B	0007565	biological_process	female pregnancy
B	0009410	biological_process	response to xenobiotic stimulus
B	0009635	biological_process	response to herbicide
B	0010042	biological_process	response to manganese ion
B	0010043	biological_process	response to zinc ion
B	0010269	biological_process	response to selenium ion
B	0014075	biological_process	response to amine
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	0030324	biological_process	lung development
B	0032496	biological_process	response to lipopolysaccharide
B	0032964	biological_process	collagen biosynthetic process
B	0033189	biological_process	response to vitamin A
B	0033197	biological_process	response to vitamin E
B	0042130	biological_process	negative regulation of T cell proliferation
B	0042802	molecular_function	identical protein binding
B	0042832	biological_process	defense response to protozoan
B	0043025	cellular_component	neuronal cell body
B	0043200	biological_process	response to amino acid
B	0043434	biological_process	response to peptide hormone
B	0045087	biological_process	innate immune response
B	0046007	biological_process	negative regulation of activated T cell proliferation
B	0046686	biological_process	response to cadmium ion
B	0046872	molecular_function	metal ion binding
B	0048545	biological_process	response to steroid hormone
B	0048678	biological_process	response to axon injury
B	0051597	biological_process	response to methylmercury
B	0060056	biological_process	mammary gland involution
B	0060135	biological_process	maternal process involved in female pregnancy
B	0060336	biological_process	negative regulation of type II interferon-mediated signaling pathway
B	0070301	biological_process	cellular response to hydrogen peroxide
B	0070965	biological_process	positive regulation of neutrophil mediated killing of fungus
B	0071222	biological_process	cellular response to lipopolysaccharide
B	0071353	biological_process	cellular response to interleukin-4
B	0071377	biological_process	cellular response to glucagon stimulus
B	0071549	biological_process	cellular response to dexamethasone stimulus
B	0071560	biological_process	cellular response to transforming growth factor beta stimulus
B	1905541	biological_process	regulation of L-arginine import across plasma membrane
B	2000552	biological_process	negative regulation of T-helper 2 cell cytokine production
C	0000050	biological_process	urea cycle
C	0001889	biological_process	liver development
C	0001938	biological_process	positive regulation of endothelial cell proliferation
C	0002250	biological_process	adaptive immune response
C	0004053	molecular_function	arginase activity
C	0005615	cellular_component	extracellular space
C	0005737	cellular_component	cytoplasm
C	0005741	cellular_component	mitochondrial outer membrane
C	0005829	cellular_component	cytosol
C	0006525	biological_process	arginine metabolic process
C	0007565	biological_process	female pregnancy
C	0009410	biological_process	response to xenobiotic stimulus
C	0009635	biological_process	response to herbicide
C	0010042	biological_process	response to manganese ion
C	0010043	biological_process	response to zinc ion
C	0010269	biological_process	response to selenium ion
C	0014075	biological_process	response to amine
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	0030324	biological_process	lung development
C	0032496	biological_process	response to lipopolysaccharide
C	0032964	biological_process	collagen biosynthetic process
C	0033189	biological_process	response to vitamin A
C	0033197	biological_process	response to vitamin E
C	0042130	biological_process	negative regulation of T cell proliferation
C	0042802	molecular_function	identical protein binding
C	0042832	biological_process	defense response to protozoan
C	0043025	cellular_component	neuronal cell body
C	0043200	biological_process	response to amino acid
C	0043434	biological_process	response to peptide hormone
C	0045087	biological_process	innate immune response
C	0046007	biological_process	negative regulation of activated T cell proliferation
C	0046686	biological_process	response to cadmium ion
C	0046872	molecular_function	metal ion binding
C	0048545	biological_process	response to steroid hormone
C	0048678	biological_process	response to axon injury
C	0051597	biological_process	response to methylmercury
C	0060056	biological_process	mammary gland involution
C	0060135	biological_process	maternal process involved in female pregnancy
C	0060336	biological_process	negative regulation of type II interferon-mediated signaling pathway
C	0070301	biological_process	cellular response to hydrogen peroxide
C	0070965	biological_process	positive regulation of neutrophil mediated killing of fungus
C	0071222	biological_process	cellular response to lipopolysaccharide
C	0071353	biological_process	cellular response to interleukin-4
C	0071377	biological_process	cellular response to glucagon stimulus
C	0071549	biological_process	cellular response to dexamethasone stimulus
C	0071560	biological_process	cellular response to transforming growth factor beta stimulus
C	1905541	biological_process	regulation of L-arginine import across plasma membrane
C	2000552	biological_process	negative regulation of T-helper 2 cell cytokine production

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN A 500

Chain	Residue
A	ASP124
A	HIS126
A	ASP232
A	ASP234

---

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN B 501

Chain	Residue
B	ASP124
B	HIS126
B	ASP232
B	ASP234

---

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN C 502

Chain	Residue
C	ASP124
C	HIS126
C	ASP232
C	ASP234

---

site_id	MNA
Number of Residues	6
Details	BI-MANGANESE NUCLEAR BINDING SITE.

Chain	Residue
A	ASN101
A	ASP124
A	HIS126
A	ASP128
A	ASP232
A	ASP234

---

site_id	MNB
Number of Residues	6
Details	BI-MANGANESE NUCLEAR BINDING SITE.

Chain	Residue
B	ASP128
B	ASP232
B	ASP234
B	ASN101
B	ASP124
B	HIS126

---

site_id	MNC
Number of Residues	6
Details	BI-MANGANESE NUCLEAR BINDING SITE.

Chain	Residue
C	ASN101
C	ASP124
C	HIS126
C	ASP128
C	ASP232
C	ASP234

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	SER230-GLY251

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269|PubMed:10542097, ECO:0000269|PubMed:12820884, ECO:0000269|PubMed:15315440, ECO:0000269|PubMed:16266687, ECO:0000269|PubMed:8849731, ECO:0007744|PDB:1D3V, ECO:0007744|PDB:1HQ5, ECO:0007744|PDB:1HQF, ECO:0007744|PDB:1HQG, ECO:0007744|PDB:1HQH, ECO:0007744|PDB:1HQX, ECO:0007744|PDB:1P8M, ECO:0007744|PDB:1P8N, ECO:0007744|PDB:1P8O, ECO:0007744|PDB:1P8Q, ECO:0007744|PDB:1P8S, ECO:0007744|PDB:1R1O, ECO:0007744|PDB:1RLA, ECO:0007744|PDB:1T4P, ECO:0007744|PDB:1T4R, ECO:0007744|PDB:1T4S, ECO:0007744|PDB:1T4T, ECO:0007744|PDB:1T5F, ECO:0007744|PDB:1T5G, ECO:0007744|PDB:1TA1, ECO:0007744|PDB:1TBH, ECO:0007744|PDB:1TBJ, ECO:0007744|PDB:1TBL, ECO:0007744|PDB:1ZPE, ECO:0007744|PDB:1ZPG, ECO:0007744|PDB:3E8Q, ECO:0007744|PDB:3E8Z, ECO:0007744|PDB:3E9B

Chain	Residue	Details
A	ASN101
B	ASN101
C	ASN101

---

site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269|PubMed:10542097, ECO:0000269|PubMed:12820884, ECO:0000269|PubMed:15315440, ECO:0000269|PubMed:16266687, ECO:0000269|PubMed:8849731, ECO:0000269|PubMed:9265637, ECO:0007744|PDB:1D3V, ECO:0007744|PDB:1HQ5, ECO:0007744|PDB:1HQF, ECO:0007744|PDB:1HQG, ECO:0007744|PDB:1HQH, ECO:0007744|PDB:1HQX, ECO:0007744|PDB:1P8M, ECO:0007744|PDB:1P8O, ECO:0007744|PDB:1P8P, ECO:0007744|PDB:1P8Q, ECO:0007744|PDB:1P8R, ECO:0007744|PDB:1P8S, ECO:0007744|PDB:1R1O, ECO:0007744|PDB:1RLA, ECO:0007744|PDB:1T4P, ECO:0007744|PDB:1T4R, ECO:0007744|PDB:1T4S, ECO:0007744|PDB:1T4T, ECO:0007744|PDB:1T5F, ECO:0007744|PDB:1T5G, ECO:0007744|PDB:1TA1, ECO:0007744|PDB:1TBH, ECO:0007744|PDB:1TBJ, ECO:0007744|PDB:1TBL, ECO:0007744|PDB:1ZPE, ECO:0007744|PDB:1ZPG, ECO:0007744|PDB:2RLA, ECO:0007744|PDB:3E8Q, ECO:0007744|PDB:3E8Z, ECO:0007744|PDB:3E9B, ECO:0007744|PDB:3RLA, ECO:0007744|PDB:4RLA, ECO:0007744|PDB:5RLA

Chain	Residue	Details
A	ASP124
A	HIS126
B	ASP124
B	HIS126
C	ASP124
C	HIS126

---

site_id	SWS_FT_FI3
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269|PubMed:10542097, ECO:0000269|PubMed:12820884, ECO:0000269|PubMed:15315440, ECO:0000269|PubMed:16266687, ECO:0000269|PubMed:8849731, ECO:0000269|PubMed:9265637, ECO:0007744|PDB:1D3V, ECO:0007744|PDB:1HQ5, ECO:0007744|PDB:1HQF, ECO:0007744|PDB:1HQG, ECO:0007744|PDB:1HQH, ECO:0007744|PDB:1HQX, ECO:0007744|PDB:1P8N, ECO:0007744|PDB:1P8P, ECO:0007744|PDB:1P8Q, ECO:0007744|PDB:1P8R, ECO:0007744|PDB:1P8S, ECO:0007744|PDB:1R1O, ECO:0007744|PDB:1RLA, ECO:0007744|PDB:1T4P, ECO:0007744|PDB:1T4R, ECO:0007744|PDB:1T4S, ECO:0007744|PDB:1T4T, ECO:0007744|PDB:1T5F, ECO:0007744|PDB:1T5G, ECO:0007744|PDB:1TA1, ECO:0007744|PDB:1TBH, ECO:0007744|PDB:1TBJ, ECO:0007744|PDB:1TBL, ECO:0007744|PDB:1ZPE, ECO:0007744|PDB:1ZPG, ECO:0007744|PDB:3E8Q, ECO:0007744|PDB:3E8Z, ECO:0007744|PDB:3E9B, ECO:0007744|PDB:3RLA

Chain	Residue	Details
A	ASP128
B	ASP128
C	ASP128

---

site_id	SWS_FT_FI4
Number of Residues	3
Details	BINDING: BINDING => ECO:0007744|PDB:1HQG, ECO:0007744|PDB:1HQH

Chain	Residue	Details
A	SER137
B	SER137
C	SER137

---

site_id	SWS_FT_FI5
Number of Residues	3
Details	BINDING: BINDING => ECO:0007744|PDB:1T5G

Chain	Residue	Details
A	ASP183
B	ASP183
C	ASP183

---

site_id	SWS_FT_FI6
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269|PubMed:10542097, ECO:0000269|PubMed:12820884, ECO:0000269|PubMed:15315440, ECO:0000269|PubMed:16266687, ECO:0000269|PubMed:8849731, ECO:0000269|PubMed:9265637, ECO:0007744|PDB:1D3V, ECO:0007744|PDB:1HQ5, ECO:0007744|PDB:1HQF, ECO:0007744|PDB:1HQG, ECO:0007744|PDB:1HQH, ECO:0007744|PDB:1HQX, ECO:0007744|PDB:1P8M, ECO:0007744|PDB:1P8O, ECO:0007744|PDB:1P8P, ECO:0007744|PDB:1P8Q, ECO:0007744|PDB:1P8R, ECO:0007744|PDB:1R1O, ECO:0007744|PDB:1RLA, ECO:0007744|PDB:1T4P, ECO:0007744|PDB:1T4R, ECO:0007744|PDB:1T4S, ECO:0007744|PDB:1T4T, ECO:0007744|PDB:1T5F, ECO:0007744|PDB:1T5G, ECO:0007744|PDB:1TA1, ECO:0007744|PDB:1TBH, ECO:0007744|PDB:1TBJ, ECO:0007744|PDB:1TBL, ECO:0007744|PDB:1ZPE, ECO:0007744|PDB:1ZPG, ECO:0007744|PDB:2RLA, ECO:0007744|PDB:3E8Q, ECO:0007744|PDB:3E8Z, ECO:0007744|PDB:3E9B, ECO:0007744|PDB:3RLA, ECO:0007744|PDB:4RLA, ECO:0007744|PDB:5RLA

Chain	Residue	Details
A	ASP232
B	ASP232
C	ASP232

---

site_id	SWS_FT_FI7
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269|PubMed:10542097, ECO:0000269|PubMed:12820884, ECO:0000269|PubMed:15315440, ECO:0000269|PubMed:16266687, ECO:0000269|PubMed:8849731, ECO:0000269|PubMed:9265637, ECO:0007744|PDB:1D3V, ECO:0007744|PDB:1HQ5, ECO:0007744|PDB:1HQF, ECO:0007744|PDB:1HQG, ECO:0007744|PDB:1HQH, ECO:0007744|PDB:1HQX, ECO:0007744|PDB:1P8M, ECO:0007744|PDB:1P8O, ECO:0007744|PDB:1P8P, ECO:0007744|PDB:1P8R, ECO:0007744|PDB:1P8S, ECO:0007744|PDB:1R1O, ECO:0007744|PDB:1RLA, ECO:0007744|PDB:1T4P, ECO:0007744|PDB:1T4R, ECO:0007744|PDB:1T4S, ECO:0007744|PDB:1T4T, ECO:0007744|PDB:1T5F, ECO:0007744|PDB:1T5G, ECO:0007744|PDB:1TA1, ECO:0007744|PDB:1TBH, ECO:0007744|PDB:1TBJ, ECO:0007744|PDB:1TBL, ECO:0007744|PDB:1ZPE, ECO:0007744|PDB:1ZPG, ECO:0007744|PDB:2RLA, ECO:0007744|PDB:3E8Q, ECO:0007744|PDB:3E8Z, ECO:0007744|PDB:3E9B, ECO:0007744|PDB:3RLA, ECO:0007744|PDB:4RLA, ECO:0007744|PDB:5RLA

Chain	Residue	Details
A	ASP234
B	ASP234
C	ASP234

---

site_id	SWS_FT_FI8
Number of Residues	3
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P53608

Chain	Residue	Details
A	THR246
B	THR246
C	THR246

---

site_id	SWS_FT_FI9
Number of Residues	3
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P78540

Chain	Residue	Details
A	GLU277
B	GLU277
C	GLU277

---

site_id	SWS_FT_FI10
Number of Residues	6
Details	MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q61176

Chain	Residue	Details
A	LYS17
A	LYS75
B	LYS17
B	LYS75
C	LYS17
C	LYS75

---

site_id	SWS_FT_FI11
Number of Residues	3
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:22673903

Chain	Residue	Details
A	SER62
B	SER62
C	SER62

---

site_id	SWS_FT_FI12
Number of Residues	3
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q61176

Chain	Residue	Details
A	SER72
B	SER72
C	SER72

---

site_id	SWS_FT_FI13
Number of Residues	6
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P05089

Chain	Residue	Details
A	SER163
A	SER217
B	SER163
B	SER217
C	SER163
C	SER217

---

site_id	SWS_FT_FI14
Number of Residues	3
Details	MOD_RES: Phosphothreonine => ECO:0007744|PubMed:22673903

Chain	Residue	Details
A	THR281
B	THR281
C	THR281

---

Catalytic Information from CSA

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

Chain	Residue	Details
A	GLU277
A	ASP128

---

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

Chain	Residue	Details
B	GLU277
B	ASP128

---

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

Chain	Residue	Details
C	GLU277
C	ASP128

---