Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3NIO

Crystal structure of Pseudomonas aeruginosa guanidinobutyrase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0006527	biological_process	L-arginine catabolic process
A	0008783	molecular_function	agmatinase activity
A	0016787	molecular_function	hydrolase activity
A	0016813	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
A	0033389	biological_process	putrescine biosynthetic process from arginine, via agmatine
A	0046872	molecular_function	metal ion binding
A	0047971	molecular_function	guanidinobutyrase activity
B	0006527	biological_process	L-arginine catabolic process
B	0008783	molecular_function	agmatinase activity
B	0016787	molecular_function	hydrolase activity
B	0016813	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
B	0033389	biological_process	putrescine biosynthetic process from arginine, via agmatine
B	0046872	molecular_function	metal ion binding
B	0047971	molecular_function	guanidinobutyrase activity
C	0006527	biological_process	L-arginine catabolic process
C	0008783	molecular_function	agmatinase activity
C	0016787	molecular_function	hydrolase activity
C	0016813	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
C	0033389	biological_process	putrescine biosynthetic process from arginine, via agmatine
C	0046872	molecular_function	metal ion binding
C	0047971	molecular_function	guanidinobutyrase activity
D	0006527	biological_process	L-arginine catabolic process
D	0008783	molecular_function	agmatinase activity
D	0016787	molecular_function	hydrolase activity
D	0016813	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
D	0033389	biological_process	putrescine biosynthetic process from arginine, via agmatine
D	0046872	molecular_function	metal ion binding
D	0047971	molecular_function	guanidinobutyrase activity
E	0006527	biological_process	L-arginine catabolic process
E	0008783	molecular_function	agmatinase activity
E	0016787	molecular_function	hydrolase activity
E	0016813	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
E	0033389	biological_process	putrescine biosynthetic process from arginine, via agmatine
E	0046872	molecular_function	metal ion binding
E	0047971	molecular_function	guanidinobutyrase activity
F	0006527	biological_process	L-arginine catabolic process
F	0008783	molecular_function	agmatinase activity
F	0016787	molecular_function	hydrolase activity
F	0016813	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
F	0033389	biological_process	putrescine biosynthetic process from arginine, via agmatine
F	0046872	molecular_function	metal ion binding
F	0047971	molecular_function	guanidinobutyrase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MN A 1601

Chain	Residue
A	HIS129
A	ASP152
A	ASP156
A	ASP243
A	HOH624
A	HOH1061
A	MN1602

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MN A 1602

Chain	Residue
A	ASP243
A	ASP245
A	HOH624
A	MN1601
A	ASP152
A	HIS154

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MN B 1603

Chain	Residue
B	HIS129
B	ASP152
B	ASP156
B	ASP243
B	HOH791
B	HOH1060
B	MN1604

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MN B 1604

Chain	Residue
B	ASP152
B	HIS154
B	ASP243
B	ASP245
B	HOH791
B	MN1603

site_id	AC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MN C 1605

Chain	Residue
C	HIS129
C	ASP152
C	ASP156
C	ASP243
C	HOH1007
C	HOH1059
C	MN1606

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MN C 1606

Chain	Residue
C	ASP152
C	HIS154
C	ASP243
C	ASP245
C	HOH1007
C	MN1605

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MN D 1607

Chain	Residue
D	HIS129
D	ASP152
D	ASP156
D	ASP243
D	HOH1040
D	HOH1058
D	MN1608

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MN D 1608

Chain	Residue
D	ASP152
D	HIS154
D	ASP243
D	ASP245
D	HOH1040
D	MN1607

site_id	AC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MN E 1609

Chain	Residue
E	HIS129
E	ASP152
E	ASP156
E	ASP243
E	HOH1033
E	HOH1057
E	MN1610

site_id	BC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MN E 1610

Chain	Residue
E	ASP152
E	HIS154
E	ASP243
E	ASP245
E	HOH1033
E	MN1609

site_id	BC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MN F 1611

Chain	Residue
F	HIS129
F	ASP152
F	ASP156
F	ASP243
F	HOH1034
F	HOH1056
F	MN1612

site_id	BC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MN F 1612

Chain	Residue
F	ASP152
F	HIS154
F	ASP243
F	ASP245
F	HOH1034
F	MN1611

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	SER241-GLY262

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	36
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00742","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21600989","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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