Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6FMS

IMISX-EP of Se-LspA

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004190	molecular_function	aspartic-type endopeptidase activity
A	0005886	cellular_component	plasma membrane
A	0006465	biological_process	signal peptide processing
A	0006508	biological_process	proteolysis
A	0008233	molecular_function	peptidase activity
A	0016020	cellular_component	membrane
A	0016787	molecular_function	hydrolase activity
B	0004190	molecular_function	aspartic-type endopeptidase activity
B	0005886	cellular_component	plasma membrane
B	0006465	biological_process	signal peptide processing
B	0006508	biological_process	proteolysis
B	0008233	molecular_function	peptidase activity
B	0016020	cellular_component	membrane
B	0016787	molecular_function	hydrolase activity
C	0004190	molecular_function	aspartic-type endopeptidase activity
C	0005886	cellular_component	plasma membrane
C	0006465	biological_process	signal peptide processing
C	0006508	biological_process	proteolysis
C	0008233	molecular_function	peptidase activity
C	0016020	cellular_component	membrane
C	0016787	molecular_function	hydrolase activity
D	0004190	molecular_function	aspartic-type endopeptidase activity
D	0005886	cellular_component	plasma membrane
D	0006465	biological_process	signal peptide processing
D	0006508	biological_process	proteolysis
D	0008233	molecular_function	peptidase activity
D	0016020	cellular_component	membrane
D	0016787	molecular_function	hydrolase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	binding site for residue OLC A 201

Chain	Residue
A	PHE29
A	ILE40
A	OLC202

site_id	AC2
Number of Residues	3
Details	binding site for residue OLC A 202

Chain	Residue
A	VAL42
A	TRP49
A	OLC201

site_id	AC3
Number of Residues	6
Details	binding site for residue OLC A 203

Chain	Residue
D	ALA28
D	ALA32
E	OLC301
A	PRO11
A	TRP12
A	ILE15

site_id	AC4
Number of Residues	6
Details	binding site for residue OLC A 204

Chain	Residue
A	PHE7
A	LEU10
A	PRO11
A	TRP14
D	GLN31
D	TYR114

site_id	AC5
Number of Residues	2
Details	binding site for residue OLC A 205

Chain	Residue
A	ARG70
A	MSE117

site_id	AC6
Number of Residues	7
Details	binding site for residue OLC B 202

Chain	Residue
B	GLY8
B	ARG9
B	PRO11
B	TRP12
B	ILE15
B	LYS93
B	LEU104

site_id	AC7
Number of Residues	3
Details	binding site for residue OLC B 203

Chain	Residue
B	LEU10
B	TRP14
C	TYR114

site_id	AC8
Number of Residues	5
Details	binding site for residue OLC B 204

Chain	Residue
A	ALA63
A	ASP64
B	TRP130
B	ARG133
B	TRP134

site_id	AC9
Number of Residues	1
Details	binding site for residue OLC B 205

Chain	Residue
B	GLU33

site_id	AD1
Number of Residues	1
Details	binding site for residue OLC B 206

Chain	Residue
B	TRP49

site_id	AD2
Number of Residues	5
Details	binding site for residue OLC C 201

Chain	Residue
C	PHE139
C	ASP143
C	THR147
G	IIL202
G	ALO204

site_id	AD3
Number of Residues	3
Details	binding site for residue OLC C 202

Chain	Residue
C	VAL41
C	TRP49
C	OLC205

site_id	AD4
Number of Residues	4
Details	binding site for residue OLC C 203

Chain	Residue
C	LEU110
C	MSE117
C	VAL118
C	OLC204

site_id	AD5
Number of Residues	3
Details	binding site for residue OLC C 204

Chain	Residue
C	ARG70
C	MSE117
C	OLC203

site_id	AD6
Number of Residues	4
Details	binding site for residue OLC C 205

Chain	Residue
C	PHE29
C	GLU33
C	TRP49
C	OLC202

site_id	AD7
Number of Residues	3
Details	binding site for residue OLC D 201

Chain	Residue
D	PHE29
D	ILE40
D	OLC202

site_id	AD8
Number of Residues	2
Details	binding site for residue OLC D 202

Chain	Residue
D	TRP49
D	OLC201

site_id	AD9
Number of Residues	7
Details	binding site for residue OLC E 301

Chain	Residue
A	PHE139
A	ASP143
A	VAL148
A	OLC203
E	IIL202
E	SER203
E	ALO204

site_id	AE1
Number of Residues	8
Details	binding site for residue OLC F 301

Chain	Residue
B	THR55
B	PRO137
B	PHE139
B	ASP143
B	THR147
F	IIL202
F	SER203
F	ALO204

site_id	AE2
Number of Residues	6
Details	binding site for residue OLC H 301

Chain	Residue
D	PHE139
D	ASP143
D	THR147
H	IIL202
H	SER203
H	ALO204

site_id	AE3
Number of Residues	9
Details	binding site for Ligand residues ALO E 204 through SER E 203 bound to SER E 203

Chain	Residue
A	ASN54
A	GLY56
A	PHE59
A	PHE73
A	ASN112
A	ARG116
A	ASP124
A	ASP143
E	OLC301

site_id	AE4
Number of Residues	12
Details	binding site for Ligand residues ALO F 204 through SER F 203 bound to SER F 203

Chain	Residue
B	ASN140
B	ASP143
B	ILE146
F	OLC301
B	LEU62
B	PHE73
B	ALA77
B	VAL80
B	ASN112
B	ARG116
B	VAL122
B	ASP124

site_id	AE5
Number of Residues	12
Details	binding site for Ligand residues ALO G 204 through SER G 203 bound to SER G 203

Chain	Residue
C	ASN54
C	PHE59
C	PHE73
C	ALA77
C	ASN112
C	ARG116
C	VAL122
C	ASP124
C	ASP143
C	ILE146
C	OLC201
H	5BV205

site_id	AE6
Number of Residues	13
Details	binding site for Ligand residues ALO H 204 through SER H 203 bound to SER H 203

Chain	Residue
D	ASN54
D	ALA57
D	PHE59
D	PHE73
D	VAL80
D	ALA109
D	ASN112
D	ARG116
D	ASP124
D	ASP143
D	ILE146
G	5BV205
H	OLC301

Functional Information from PROSITE/UniProt

site_id	PS00855
Number of Residues	13
Details	SPASE_II Signal peptidases II signature. VlGGALGNLYDRM

Chain	Residue	Details
A	VAL105-MSE117

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	80
Details	TRANSMEM: Helical => ECO:0000255\|HAMAP-Rule:MF_00161, ECO:0000269\|PubMed:26912896, ECO:0000269\|PubMed:30272004, ECO:0007744\|PDB:5DIR, ECO:0007744\|PDB:6FMS

Chain	Residue	Details
A	LEU10-PHE30
B	LEU10-PHE30
C	LEU10-PHE30
D	LEU10-PHE30

site_id	SWS_FT_FI2
Number of Residues	228
Details	TOPO_DOM: Periplasmic => ECO:0000269\|PubMed:26912896, ECO:0000269\|PubMed:30272004, ECO:0007744\|PDB:5DIR, ECO:0007744\|PDB:6FMS

Chain	Residue	Details
A	GLN31-GLY67
A	LEU119-ASN140
B	GLN31-GLY67
B	LEU119-ASN140
C	GLN31-GLY67
C	LEU119-ASN140
D	GLN31-GLY67
D	LEU119-ASN140

site_id	SWS_FT_FI3
Number of Residues	168
Details	TRANSMEM: Helical => ECO:0000269\|PubMed:26912896, ECO:0000269\|PubMed:30272004, ECO:0007744\|PDB:5DIR, ECO:0007744\|PDB:6FMS

Chain	Residue	Details
A	TRP68-LYS89
A	TRP97-VAL118
B	TRP68-LYS89
B	TRP97-VAL118
C	TRP68-LYS89
C	TRP97-VAL118
D	TRP68-LYS89
D	TRP97-VAL118

site_id	SWS_FT_FI4
Number of Residues	24
Details	TOPO_DOM: Cytoplasmic => ECO:0000269\|PubMed:26912896, ECO:0000269\|PubMed:30272004, ECO:0007744\|PDB:5DIR, ECO:0007744\|PDB:6FMS

Chain	Residue	Details
A	ARG90-THR96
B	ARG90-THR96
C	ARG90-THR96
D	ARG90-THR96

site_id	SWS_FT_FI5
Number of Residues	52
Details	TRANSMEM: Helical => ECO:0000269\|PubMed:26912896, ECO:0007744\|PDB:5DIR

Chain	Residue	Details
A	LEU141-ALA154
B	LEU141-ALA154
C	LEU141-ALA154
D	LEU141-ALA154

site_id	SWS_FT_FI6
Number of Residues	56
Details	TOPO_DOM: Cytoplasmic => ECO:0000269\|PubMed:26912896, ECO:0007744\|PDB:5DIR

Chain	Residue	Details
A	LEU155-GLY169
B	LEU155-GLY169
C	LEU155-GLY169
D	LEU155-GLY169

site_id	SWS_FT_FI7
Number of Residues	8
Details	ACT_SITE: ACT_SITE => ECO:0000255\|HAMAP-Rule:MF_00161, ECO:0000305\|PubMed:26912896

Chain	Residue	Details
A	ASP124
A	ASP143
B	ASP124
B	ASP143
C	ASP124
C	ASP143
D	ASP124
D	ASP143

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