Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3M1R

The crystal structure of formimidoylglutamase from Bacillus subtilis subsp. subtilis str. 168

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0006547	biological_process	L-histidine metabolic process
A	0006548	biological_process	L-histidine 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	0019556	biological_process	obsolete L-histidine catabolic process to glutamate and formamide
A	0019557	biological_process	obsolete L-histidine catabolic process to glutamate and formate
A	0030145	molecular_function	manganese ion binding
A	0033389	biological_process	putrescine biosynthetic process from arginine, via agmatine
A	0046872	molecular_function	metal ion binding
A	0050415	molecular_function	formimidoylglutamase activity
B	0006547	biological_process	L-histidine metabolic process
B	0006548	biological_process	L-histidine 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	0019556	biological_process	obsolete L-histidine catabolic process to glutamate and formamide
B	0019557	biological_process	obsolete L-histidine catabolic process to glutamate and formate
B	0030145	molecular_function	manganese ion binding
B	0033389	biological_process	putrescine biosynthetic process from arginine, via agmatine
B	0046872	molecular_function	metal ion binding
B	0050415	molecular_function	formimidoylglutamase activity
C	0006547	biological_process	L-histidine metabolic process
C	0006548	biological_process	L-histidine 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	0019556	biological_process	obsolete L-histidine catabolic process to glutamate and formamide
C	0019557	biological_process	obsolete L-histidine catabolic process to glutamate and formate
C	0030145	molecular_function	manganese ion binding
C	0033389	biological_process	putrescine biosynthetic process from arginine, via agmatine
C	0046872	molecular_function	metal ion binding
C	0050415	molecular_function	formimidoylglutamase activity
D	0006547	biological_process	L-histidine metabolic process
D	0006548	biological_process	L-histidine 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	0019556	biological_process	obsolete L-histidine catabolic process to glutamate and formamide
D	0019557	biological_process	obsolete L-histidine catabolic process to glutamate and formate
D	0030145	molecular_function	manganese ion binding
D	0033389	biological_process	putrescine biosynthetic process from arginine, via agmatine
D	0046872	molecular_function	metal ion binding
D	0050415	molecular_function	formimidoylglutamase activity
E	0006547	biological_process	L-histidine metabolic process
E	0006548	biological_process	L-histidine 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	0019556	biological_process	obsolete L-histidine catabolic process to glutamate and formamide
E	0019557	biological_process	obsolete L-histidine catabolic process to glutamate and formate
E	0030145	molecular_function	manganese ion binding
E	0033389	biological_process	putrescine biosynthetic process from arginine, via agmatine
E	0046872	molecular_function	metal ion binding
E	0050415	molecular_function	formimidoylglutamase activity
F	0006547	biological_process	L-histidine metabolic process
F	0006548	biological_process	L-histidine 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	0019556	biological_process	obsolete L-histidine catabolic process to glutamate and formamide
F	0019557	biological_process	obsolete L-histidine catabolic process to glutamate and formate
F	0030145	molecular_function	manganese ion binding
F	0033389	biological_process	putrescine biosynthetic process from arginine, via agmatine
F	0046872	molecular_function	metal ion binding
F	0050415	molecular_function	formimidoylglutamase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL A 320

Chain	Residue
A	ASN127
A	ASP154
A	CA322

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL A 321

Chain	Residue
A	HIS51
A	THR291
D	HIS51

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 322

Chain	Residue
A	ASP244
A	CL320
A	CA323
A	ASP150
A	HIS152
A	ASP242

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA A 323

Chain	Residue
A	ASN127
A	ASP150
A	ASP154
A	ASP242
A	CA322

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PEG A 324

Chain	Residue
A	SER55
A	PHE56
A	PRO58
A	GLY59
A	THR60

site_id	AC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PEG A 325

Chain	Residue
A	GLU190
A	PHE191
A	PRO259
A	PEG326
B	ASP265
B	HIS304
B	HIS308

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PEG A 326

Chain	Residue
A	MSE211
A	ASP212
A	ARG215
A	GLY260
A	PEG325

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL B 320

Chain	Residue
B	ASP154
B	CA322
B	CA323

site_id	AC9
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CL B 321

Chain	Residue
B	HIS51
E	HIS51

site_id	BC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA B 322

Chain	Residue
B	ASP150
B	HIS152
B	ASP242
B	ASP244
B	CL320
B	CA323

site_id	BC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA B 323

Chain	Residue
B	ASN127
B	ASP150
B	ASP154
B	ASP242
B	CL320
B	CA322

site_id	BC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PEG B 324

Chain	Residue
B	ALA151
B	HIS152
B	ARG189
B	SER192
B	ASP244
B	ALA256

site_id	BC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PEG B 325

Chain	Residue
B	ARG295
B	ASP296
B	HOH327

site_id	BC5
Number of Residues	10
Details	BINDING SITE FOR RESIDUE CAC C 320

Chain	Residue
A	SER249
A	PRO252
A	PHE294
A	MSE297
B	SER249
B	PHE294
C	SER249
C	PRO252
C	PHE294
C	MSE297

site_id	BC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL C 321

Chain	Residue
C	HIS152
C	ASP154
C	CA323
C	CA324

site_id	BC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL C 322

Chain	Residue
C	HIS51
C	THR291
F	HIS51

site_id	BC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA C 323

Chain	Residue
C	ASP150
C	HIS152
C	ASP242
C	ASP244
C	CL321
C	CA324

site_id	BC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA C 324

Chain	Residue
C	ASN127
C	ASP150
C	ASP154
C	ASP242
C	CL321
C	CA323

site_id	CC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PEG C 325

Chain	Residue
C	GLY31
F	LYS224

site_id	CC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PEG C 326

Chain	Residue
C	SER23
C	ILE26
C	LYS66
C	ASP86

site_id	CC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PEG C 327

Chain	Residue
C	ASP244
C	ALA256
C	ALA151
C	HIS152
C	ARG189
C	SER192

site_id	CC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PEG C 328

Chain	Residue
B	GLU190
B	PRO259
B	GLY260
C	ASP265
C	HIS304
C	HIS308

site_id	CC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PEG C 329

Chain	Residue
C	PRO116
C	LYS141
C	PHE236
C	VAL280

site_id	CC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PEG C 330

Chain	Residue
C	ASP265
C	GLU266

site_id	CC7
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PEG C 331

Chain	Residue
C	SER55
E	SER12

site_id	CC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL D 320

Chain	Residue
D	ASP154
D	CA321
D	CA322

site_id	CC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA D 321

Chain	Residue
D	ASP150
D	HIS152
D	ASP242
D	ASP244
D	CL320
D	CA322

site_id	DC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA D 322

Chain	Residue
D	ASN127
D	ASP150
D	ASP154
D	ASP242
D	CL320
D	CA321

site_id	DC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PEG D 323

Chain	Residue
D	ALA151
D	HIS152
D	ARG189
D	SER192
D	ASP244
D	ALA256
D	HOH352

site_id	DC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PEG D 324

Chain	Residue
D	GLU269
D	HIS304
D	HIS308
E	GLU190
E	PHE191
E	PRO259

site_id	DC4
Number of Residues	11
Details	BINDING SITE FOR RESIDUE CAC E 320

Chain	Residue
D	SER249
D	PHE294
D	MSE297
E	SER249
E	PRO252
E	PHE294
E	MSE297
F	SER249
F	PRO252
F	PHE294
F	MSE297

site_id	DC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL E 321

Chain	Residue
E	ASP154
E	CA322
E	CA323

site_id	DC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA E 322

Chain	Residue
E	ASP150
E	HIS152
E	ASP242
E	ASP244
E	CL321
E	CA323

site_id	DC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA E 323

Chain	Residue
E	ASN127
E	ASP150
E	ASP154
E	ASP242
E	CL321
E	CA322

site_id	DC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PEG E 324

Chain	Residue
E	ALA151
E	HIS152
E	ARG189
E	SER192
E	ASP244
E	ALA256
E	HOH355

site_id	DC9
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PEG E 325

Chain	Residue
E	ASP293
E	ARG295

site_id	EC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PEG E 326

Chain	Residue
E	ASP265
E	HIS304
E	HIS308
F	GLU190
F	PHE191
F	PRO259

site_id	EC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL F 320

Chain	Residue
F	ASP154
F	CA321
F	CA322

site_id	EC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA F 321

Chain	Residue
F	ASP150
F	HIS152
F	ASP242
F	ASP244
F	CL320
F	CA322

site_id	EC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA F 322

Chain	Residue
F	ASN127
F	ASP150
F	ASP154
F	ASP242
F	CL320
F	CA321

site_id	EC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PEG F 323

Chain	Residue
D	LEU292
F	PHE294
F	ARG295
F	HOH349

site_id	EC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PEG F 324

Chain	Residue
D	GLU190
D	PHE191
D	GLY260
F	ASP265
F	GLU269
F	HIS304
F	HIS308

site_id	EC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PEG F 325

Chain	Residue
A	LEU7
F	TRP29
F	ASP86
F	LEU87

site_id	EC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PEG F 326

Chain	Residue
F	PRO43
F	ILE92

site_id	EC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PEG F 327

Chain	Residue
F	ASP232
F	THR234
F	ASP235

site_id	FC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PEG F 328

Chain	Residue
F	ALA151
F	HIS152
F	ARG189
F	SER192
F	ASP244
F	ALA256
F	HOH346

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	SER240-GLY261

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	35
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00737","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"MAR-2010","submissionDatabase":"PDB data bank","title":"The crystal structure of formimidoylglutamase from Bacillus subtilis subsp. subtilis str. 168.","authors":["Tan K.","Bigelow L.","Buck K.","Joachimiak A."]}}]}

Chain

Residue

Details

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