Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4GSZ

Crystal Structure of the Zn2+5-Human Arginase I-ABH Complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000050	biological_process	urea cycle
A	0002250	biological_process	adaptive immune response
A	0004053	molecular_function	arginase activity
A	0005515	molecular_function	protein binding
A	0005576	cellular_component	extracellular region
A	0005615	cellular_component	extracellular space
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006525	biological_process	arginine metabolic process
A	0006527	biological_process	arginine catabolic 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	0035578	cellular_component	azurophil granule lumen
A	0035580	cellular_component	specific granule lumen
A	0042130	biological_process	negative regulation of T cell proliferation
A	0042832	biological_process	defense response to protozoan
A	0045087	biological_process	innate immune response
A	0046007	biological_process	negative regulation of activated T cell proliferation
A	0046872	molecular_function	metal ion binding
A	0060336	biological_process	negative regulation of type II interferon-mediated signaling pathway
A	0070965	biological_process	positive regulation of neutrophil mediated killing of fungus
A	2000552	biological_process	negative regulation of T-helper 2 cell cytokine production
B	0000050	biological_process	urea cycle
B	0002250	biological_process	adaptive immune response
B	0004053	molecular_function	arginase activity
B	0005515	molecular_function	protein binding
B	0005576	cellular_component	extracellular region
B	0005615	cellular_component	extracellular space
B	0005634	cellular_component	nucleus
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006525	biological_process	arginine metabolic process
B	0006527	biological_process	arginine catabolic 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	0035578	cellular_component	azurophil granule lumen
B	0035580	cellular_component	specific granule lumen
B	0042130	biological_process	negative regulation of T cell proliferation
B	0042832	biological_process	defense response to protozoan
B	0045087	biological_process	innate immune response
B	0046007	biological_process	negative regulation of activated T cell proliferation
B	0046872	molecular_function	metal ion binding
B	0060336	biological_process	negative regulation of type II interferon-mediated signaling pathway
B	0070965	biological_process	positive regulation of neutrophil mediated killing of fungus
B	2000552	biological_process	negative regulation of T-helper 2 cell cytokine production

Functional Information from PDB Data

site_id	AC1
Number of Residues	1
Details	BINDING SITE FOR RESIDUE ZN A 401

Chain	Residue
A	HIS312

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ZN A 402

Chain	Residue
A	HIS101
A	ASP124
A	ASP128
A	ASP232
A	ZN403
A	ABH405

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ZN A 403

Chain	Residue
A	ASP232
A	ASP234
A	ZN402
A	ABH405
A	ASP124
A	HIS126

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 404

Chain	Residue
A	HIS141
A	GLU277
A	ABH405
A	HOH559

site_id	AC5
Number of Residues	19
Details	BINDING SITE FOR RESIDUE ABH A 405

Chain	Residue
A	HIS101
A	ASP124
A	HIS126
A	ASP128
A	ASN130
A	SER137
A	HIS141
A	GLY142
A	ASP183
A	GLU186
A	ASP232
A	ASP234
A	THR246
A	GLU277
A	ZN402
A	ZN403
A	ZN404
A	HOH506
A	HOH558

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 406

Chain	Residue
A	HIS115
A	ASP117
A	PRO226
A	HOH560

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ZN B 401

Chain	Residue
B	HIS101
B	ASP124
B	ASP128
B	ASP232
B	ZN402
B	ABH403

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ZN B 402

Chain	Residue
B	ASP124
B	HIS126
B	ASP232
B	ASP234
B	ZN401
B	ABH403

site_id	AC9
Number of Residues	21
Details	BINDING SITE FOR RESIDUE ABH B 403

Chain	Residue
B	HIS101
B	ASP124
B	HIS126
B	ASP128
B	ASN130
B	SER137
B	HIS141
B	GLY142
B	ASP183
B	ASP232
B	ASP234
B	THR246
B	GLU277
B	ZN401
B	ZN402
B	ZN404
B	HOH502
B	HOH505
B	HOH525
B	HOH538
B	HOH541

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 404

Chain	Residue
B	HIS141
B	GLU277
B	ABH403
B	HOH538

site_id	BC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ZN B 405

Chain	Residue
B	HIS115
B	ASP117
B	HOH543

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	SER230-GLY251

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269\|PubMed:16141327, ECO:0000269\|PubMed:17469833, ECO:0000269\|PubMed:17562323, ECO:0000269\|PubMed:18802628, ECO:0000269\|PubMed:21728378, ECO:0007744\|PDB:1WVA, ECO:0007744\|PDB:1WVB, ECO:0007744\|PDB:2AEB, ECO:0007744\|PDB:2PHA, ECO:0007744\|PDB:2PHO, ECO:0007744\|PDB:2PLL, ECO:0007744\|PDB:2ZAV, ECO:0007744\|PDB:3DJ8, ECO:0007744\|PDB:3E6K, ECO:0007744\|PDB:3E6V, ECO:0007744\|PDB:3F80, ECO:0007744\|PDB:3GMZ, ECO:0007744\|PDB:3GN0, ECO:0007744\|PDB:3KV2, ECO:0007744\|PDB:3LP4, ECO:0007744\|PDB:3LP7, ECO:0007744\|PDB:3MFV, ECO:0007744\|PDB:3MFW, ECO:0007744\|PDB:3MJL, ECO:0007744\|PDB:3SJT, ECO:0007744\|PDB:3SKK, ECO:0007744\|PDB:4FCI, ECO:0007744\|PDB:4GSZ, ECO:0007744\|PDB:4GWC, ECO:0007744\|PDB:4GWD, ECO:0007744\|PDB:4HWW, ECO:0007744\|PDB:4HXQ, ECO:0007744\|PDB:4IE1

Chain	Residue	Details
A	HIS101
B	ASP128
B	ASP232
B	ASP234
A	ASP124
A	HIS126
A	ASP128
A	ASP232
A	ASP234
B	HIS101
B	ASP124
B	HIS126

site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0007744\|PDB:3GMZ, ECO:0007744\|PDB:3GN0, ECO:0007744\|PDB:3KV2, ECO:0007744\|PDB:3LP7, ECO:0007744\|PDB:3THJ

Chain	Residue	Details
A	SER137
A	ASP183
B	SER137
B	ASP183

site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000250\|UniProtKB:P53608

Chain	Residue	Details
A	THR246
B	THR246

site_id	SWS_FT_FI4
Number of Residues	2
Details	BINDING: BINDING => ECO:0000250\|UniProtKB:P78540

Chain	Residue	Details
A	GLU277
B	GLU277

site_id	SWS_FT_FI5
Number of Residues	4
Details	MOD_RES: N6-succinyllysine => ECO:0000250\|UniProtKB:Q61176

Chain	Residue	Details
A	LYS17
A	LYS75
B	LYS17
B	LYS75

site_id	SWS_FT_FI6
Number of Residues	6
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:24275569

Chain	Residue	Details
A	SER62
A	SER163
A	SER217
B	SER62
B	SER163
B	SER217

site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000250\|UniProtKB:Q61176

Chain	Residue	Details
A	SER72
B	SER72

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