6NC9

Lipid II flippase MurJ, outward-facing conformation

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005886	cellular_component	plasma membrane
A	0008360	biological_process	regulation of cell shape
A	0009252	biological_process	peptidoglycan biosynthetic process
A	0015648	molecular_function	lipid-linked peptidoglycan transporter activity
A	0015836	biological_process	lipid-linked peptidoglycan transport
A	0034204	biological_process	lipid translocation
A	0071555	biological_process	cell wall organization

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	binding site for residue 1PE A 501

Chain	Residue
A	TYR285
A	ASN288
A	ASP289
A	LYS292
A	ASP416
A	OLB506

---

site_id	AC2
Number of Residues	9
Details	binding site for residue OLB A 502

Chain	Residue
A	LEU126
A	PRO130
A	ILE178
A	OLC511
A	HOH606
A	HOH716
A	TYR36
A	GLU37
A	LYS123

---

site_id	AC3
Number of Residues	8
Details	binding site for residue OLB A 503

Chain	Residue
A	ILE306
A	PHE307
A	SER309
A	THR310
A	PRO311
A	SER331
A	OLC515
A	HOH605

---

site_id	AC4
Number of Residues	8
Details	binding site for residue OLB A 504

Chain	Residue
A	LYS419
A	PHE461
A	TYR462
A	ARG463
A	ASP464
A	LEU465
A	HOH604
A	HOH751

---

site_id	AC5
Number of Residues	7
Details	binding site for residue OLB A 505

Chain	Residue
A	ALA93
A	ILE208
A	PHE211
A	PRO212
A	PHE241
A	ILE379
A	OLC512

---

site_id	AC6
Number of Residues	8
Details	binding site for residue OLB A 506

Chain	Residue
A	LEU4
A	ASP289
A	THR293
A	PHE296
A	TYR462
A	LEU465
A	1PE501
A	OLC510

---

site_id	AC7
Number of Residues	5
Details	binding site for residue OLB A 507

Chain	Residue
A	THR164
A	GLY168
A	TYR175
A	SER179
A	OLC511

---

site_id	AC8
Number of Residues	7
Details	binding site for residue OLB A 508

Chain	Residue
A	ILE43
A	ALA44
A	MET46
A	PHE47
A	PRO48
A	ILE106
A	ILE132

---

site_id	AC9
Number of Residues	6
Details	binding site for residue NA A 509

Chain	Residue
A	ASP235
A	ASN374
A	ASP378
A	VAL390
A	ALA393
A	THR394

---

site_id	AD1
Number of Residues	5
Details	binding site for residue OLC A 510

Chain	Residue
A	SER2
A	PHE5
A	LEU465
A	PHE469
A	OLB506

---

site_id	AD2
Number of Residues	4
Details	binding site for residue OLC A 511

Chain	Residue
A	ILE178
A	TYR385
A	OLB502
A	OLB507

---

site_id	AD3
Number of Residues	4
Details	binding site for residue OLC A 512

Chain	Residue
A	ILE379
A	ILE380
A	LEU383
A	OLB505

---

site_id	AD4
Number of Residues	5
Details	binding site for residue OLC A 513

Chain	Residue
A	TRP153
A	THR157
A	ILE160
A	SER194
A	HOH693

---

site_id	AD5
Number of Residues	1
Details	binding site for residue OLC A 515

Chain	Residue
A	OLB503

---

site_id	AD6
Number of Residues	3
Details	binding site for residue OLC A 516

Chain	Residue
A	MET46
A	PHE50
A	PHE109

---

site_id	AD7
Number of Residues	7
Details	binding site for residue OLC A 517

Chain	Residue
A	ASN85
A	SER88
A	LEU89
A	LEU92
A	PHE206
A	THR207
A	ILE208

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	87
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"28024149","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	285
Details	Transmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"28024149","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	74
Details	Topological domain: {"description":"Periplasmic","evidences":[{"source":"PubMed","id":"28024149","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---