Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6OYZ

Crystal structure of MraY bound to capuramycin

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005886	cellular_component	plasma membrane
A	0007049	biological_process	cell cycle
A	0008360	biological_process	regulation of cell shape
A	0008963	molecular_function	phospho-N-acetylmuramoyl-pentapeptide-transferase activity
A	0009252	biological_process	peptidoglycan biosynthetic process
A	0016020	cellular_component	membrane
A	0016740	molecular_function	transferase activity
A	0016780	molecular_function	phosphotransferase activity, for other substituted phosphate groups
A	0042802	molecular_function	identical protein binding
A	0044038	biological_process	cell wall macromolecule biosynthetic process
A	0046872	molecular_function	metal ion binding
A	0051301	biological_process	cell division
A	0051992	molecular_function	UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine:undecaprenyl-phosphate transferase activity
A	0071555	biological_process	cell wall organization
B	0005886	cellular_component	plasma membrane
B	0007049	biological_process	cell cycle
B	0008360	biological_process	regulation of cell shape
B	0008963	molecular_function	phospho-N-acetylmuramoyl-pentapeptide-transferase activity
B	0009252	biological_process	peptidoglycan biosynthetic process
B	0016020	cellular_component	membrane
B	0016740	molecular_function	transferase activity
B	0016780	molecular_function	phosphotransferase activity, for other substituted phosphate groups
B	0042802	molecular_function	identical protein binding
B	0044038	biological_process	cell wall macromolecule biosynthetic process
B	0046872	molecular_function	metal ion binding
B	0051301	biological_process	cell division
B	0051992	molecular_function	UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine:undecaprenyl-phosphate transferase activity
B	0071555	biological_process	cell wall organization
C	0005886	cellular_component	plasma membrane
C	0007049	biological_process	cell cycle
C	0008360	biological_process	regulation of cell shape
C	0008963	molecular_function	phospho-N-acetylmuramoyl-pentapeptide-transferase activity
C	0009252	biological_process	peptidoglycan biosynthetic process
C	0016020	cellular_component	membrane
C	0016740	molecular_function	transferase activity
C	0016780	molecular_function	phosphotransferase activity, for other substituted phosphate groups
C	0042802	molecular_function	identical protein binding
C	0044038	biological_process	cell wall macromolecule biosynthetic process
C	0046872	molecular_function	metal ion binding
C	0051301	biological_process	cell division
C	0051992	molecular_function	UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine:undecaprenyl-phosphate transferase activity
C	0071555	biological_process	cell wall organization
D	0005886	cellular_component	plasma membrane
D	0007049	biological_process	cell cycle
D	0008360	biological_process	regulation of cell shape
D	0008963	molecular_function	phospho-N-acetylmuramoyl-pentapeptide-transferase activity
D	0009252	biological_process	peptidoglycan biosynthetic process
D	0016020	cellular_component	membrane
D	0016740	molecular_function	transferase activity
D	0016780	molecular_function	phosphotransferase activity, for other substituted phosphate groups
D	0042802	molecular_function	identical protein binding
D	0044038	biological_process	cell wall macromolecule biosynthetic process
D	0046872	molecular_function	metal ion binding
D	0051301	biological_process	cell division
D	0051992	molecular_function	UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine:undecaprenyl-phosphate transferase activity
D	0071555	biological_process	cell wall organization

Functional Information from PDB Data

site_id	AC1
Number of Residues	11
Details	binding site for residue NKM A 401

Chain	Residue
A	LYS70
A	GLY264
A	ASP265
A	THR75
A	LYS121
A	ASP193
A	GLY194
A	LEU195
A	ASP196
A	PHE262
A	MET263

Functional Information from PROSITE/UniProt

site_id	PS01347
Number of Residues	13
Details	MRAY_1 MraY family signature 1. KkyTPTMGGIvIL

Chain	Residue	Details
A	LYS70-LEU82

site_id	PS01348
Number of Residues	12
Details	MRAY_2 MraY family signature 2. NavNlTDGLDGL

Chain	Residue	Details
A	ASN187-LEU198

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	272
Details	TOPO_DOM: Periplasmic => ECO:0000269\|PubMed:23990562

Chain	Residue	Details
A	MET1-ARG25
C	HIS219-TYR233
C	LEU281-SER284
C	LEU356-ARG359
B	MET1-ARG25
B	MET93-LYS98
B	ASP153-VAL172
B	HIS219-TYR233
B	LEU281-SER284
B	LEU356-ARG359
D	MET1-ARG25
A	MET93-LYS98
D	MET93-LYS98
D	ASP153-VAL172
D	HIS219-TYR233
D	LEU281-SER284
D	LEU356-ARG359
A	ASP153-VAL172
A	HIS219-TYR233
A	LEU281-SER284
A	LEU356-ARG359
C	MET1-ARG25
C	MET93-LYS98
C	ASP153-VAL172

site_id	SWS_FT_FI2
Number of Residues	88
Details	TRANSMEM: Helical; Name=Helix 1 => ECO:0000269\|PubMed:23990562

Chain	Residue	Details
A	SER26-LEU48
C	SER26-LEU48
B	SER26-LEU48
D	SER26-LEU48

site_id	SWS_FT_FI3
Number of Residues	260
Details	TOPO_DOM: Cytoplasmic => ECO:0000269\|PubMed:23990562

Chain	Residue	Details
A	ARG49-PRO74
C	TRP311-LEU332
B	ARG49-PRO74
B	LYS121-ILE130
B	LEU195-GLY197
B	SER256-GLY264
B	TRP311-LEU332
D	ARG49-PRO74
D	LYS121-ILE130
D	LEU195-GLY197
D	SER256-GLY264
A	LYS121-ILE130
D	TRP311-LEU332
A	LEU195-GLY197
A	SER256-GLY264
A	TRP311-LEU332
C	ARG49-PRO74
C	LYS121-ILE130
C	LEU195-GLY197
C	SER256-GLY264

site_id	SWS_FT_FI4
Number of Residues	68
Details	TRANSMEM: Helical; Name=Helix 2 => ECO:0000269\|PubMed:23990562

Chain	Residue	Details
A	THR75-LEU92
C	THR75-LEU92
B	THR75-LEU92
D	THR75-LEU92

site_id	SWS_FT_FI5
Number of Residues	84
Details	TRANSMEM: Helical; Name=Helix 3 => ECO:0000269\|PubMed:23990562

Chain	Residue	Details
A	TYR99-VAL120
C	TYR99-VAL120
B	TYR99-VAL120
D	TYR99-VAL120

site_id	SWS_FT_FI6
Number of Residues	84
Details	TRANSMEM: Helical; Name=Helix 4 => ECO:0000269\|PubMed:23990562

Chain	Residue	Details
A	LYS131-ALA152
C	LYS131-ALA152
B	LYS131-ALA152
D	LYS131-ALA152

site_id	SWS_FT_FI7
Number of Residues	84
Details	TRANSMEM: Helical; Name=Helix 5 => ECO:0000269\|PubMed:23990562

Chain	Residue	Details
A	LEU173-GLY194
C	LEU173-GLY194
B	LEU173-GLY194
D	LEU173-GLY194

site_id	SWS_FT_FI8
Number of Residues	80
Details	TRANSMEM: Helical; Name=Helix 6 => ECO:0000269\|PubMed:23990562

Chain	Residue	Details
A	LEU198-GLY218
C	LEU198-GLY218
B	LEU198-GLY218
D	LEU198-GLY218

site_id	SWS_FT_FI9
Number of Residues	84
Details	TRANSMEM: Helical; Name=Helix 7 => ECO:0000269\|PubMed:23990562

Chain	Residue	Details
A	ALA234-ASN255
C	ALA234-ASN255
B	ALA234-ASN255
D	ALA234-ASN255

site_id	SWS_FT_FI10
Number of Residues	60
Details	TRANSMEM: Helical; Name=Helix 8 => ECO:0000269\|PubMed:23990562

Chain	Residue	Details
A	ASP265-LEU280
C	ASP265-LEU280
B	ASP265-LEU280
D	ASP265-LEU280

site_id	SWS_FT_FI11
Number of Residues	100
Details	TRANSMEM: Helical; Name=Helix 9 => ECO:0000269\|PubMed:23990562

Chain	Residue	Details
A	GLU285-ARG310
C	GLU285-ARG310
B	GLU285-ARG310
D	GLU285-ARG310

site_id	SWS_FT_FI12
Number of Residues	88
Details	TRANSMEM: Helical; Name=Helix 10 => ECO:0000269\|PubMed:23990562

Chain	Residue	Details
A	PRO333-MET355
C	PRO333-MET355
B	PRO333-MET355
D	PRO333-MET355

site_id	SWS_FT_FI13
Number of Residues	36
Details	BINDING: BINDING => ECO:0000269\|PubMed:27088606, ECO:0007744\|PDB:5CKR

Chain	Residue	Details
A	LYS70
C	LYS70
C	THR75
C	ASN190
C	ASP193
C	ASP196
C	GLY264
C	SER268
C	GLN305
C	ALA321
B	LYS70
A	THR75
B	THR75
B	ASN190
B	ASP193
B	ASP196
B	GLY264
B	SER268
B	GLN305
B	ALA321
D	LYS70
D	THR75
A	ASN190
D	ASN190
D	ASP193
D	ASP196
D	GLY264
D	SER268
D	GLN305
D	ALA321
A	ASP193
A	ASP196
A	GLY264
A	SER268
A	GLN305
A	ALA321

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