6OYH

Crystal structure of MraY bound to carbacaprazamycin

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005886	cellular_component	plasma membrane
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	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	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	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	15
Details	binding site for residue NK4 A 401

Chain	Residue
A	LYS70
A	PHE262
A	MET263
A	GLY264
A	SER268
A	HIS324
A	HIS325
A	THR75
A	ASN187
A	ASN190
A	LEU191
A	ASP193
A	GLY194
A	LEU195
A	ASP196

---

site_id	AC2
Number of Residues	17
Details	binding site for residue NK4 C 401

Chain	Residue
C	LYS70
C	THR75
C	GLY184
C	ASN187
C	ASN190
C	ASP193
C	GLY194
C	LEU195
C	ASP196
C	PHE262
C	MET263
C	GLY264
C	ASP265
C	THR299
C	PRO322
C	HIS324
C	HIS325

---

site_id	AC3
Number of Residues	14
Details	binding site for residue NK4 B 401

Chain	Residue
B	LYS70
B	THR75
B	ASP193
B	GLY194
B	LEU195
B	ASP196
B	PHE262
B	GLY264
B	SER268
B	THR299
B	ARG320
B	PRO322
B	HIS324
B	HIS325

---

site_id	AC4
Number of Residues	16
Details	binding site for residue NK4 D 401

Chain	Residue
D	LYS70
D	THR75
D	PHE180
D	ASN190
D	ASP193
D	GLY194
D	LEU195
D	ASP196
D	ASN255
D	PHE262
D	MET263
D	GLY264
D	ASP265
D	PRO322
D	HIS324
D	HIS325

---

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	88
Details	Transmembrane: {"description":"Helical; Name=Helix 1","evidences":[{"source":"PubMed","id":"23990562","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	68
Details	Transmembrane: {"description":"Helical; Name=Helix 2","evidences":[{"source":"PubMed","id":"23990562","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	164
Details	Topological domain: {"description":"Periplasmic","evidences":[{"source":"PubMed","id":"23990562","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	84
Details	Transmembrane: {"description":"Helical; Name=Helix 3","evidences":[{"source":"PubMed","id":"23990562","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	139
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"23990562","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	84
Details	Transmembrane: {"description":"Helical; Name=Helix 4","evidences":[{"source":"PubMed","id":"23990562","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	84
Details	Transmembrane: {"description":"Helical; Name=Helix 5","evidences":[{"source":"PubMed","id":"23990562","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	80
Details	Transmembrane: {"description":"Helical; Name=Helix 6","evidences":[{"source":"PubMed","id":"23990562","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	84
Details	Transmembrane: {"description":"Helical; Name=Helix 7","evidences":[{"source":"PubMed","id":"23990562","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI10
Number of Residues	60
Details	Transmembrane: {"description":"Helical; Name=Helix 8","evidences":[{"source":"PubMed","id":"23990562","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI11
Number of Residues	100
Details	Transmembrane: {"description":"Helical; Name=Helix 9","evidences":[{"source":"PubMed","id":"23990562","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI12
Number of Residues	88
Details	Transmembrane: {"description":"Helical; Name=Helix 10","evidences":[{"source":"PubMed","id":"23990562","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI13
Number of Residues	36
Details	Binding site: {"evidences":[{"source":"PubMed","id":"27088606","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5CKR","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---