6L07

Crystal structure of Escherichia coli phosphatidylserine decarboxylase (PE-bound form)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004609	molecular_function	phosphatidylserine decarboxylase activity
A	0008654	biological_process	phospholipid biosynthetic process
B	0004609	molecular_function	phosphatidylserine decarboxylase activity
B	0008654	biological_process	phospholipid biosynthetic process
C	0004609	molecular_function	phosphatidylserine decarboxylase activity
C	0008654	biological_process	phospholipid biosynthetic process
D	0004609	molecular_function	phosphatidylserine decarboxylase activity
D	0008654	biological_process	phospholipid biosynthetic process
E	0004609	molecular_function	phosphatidylserine decarboxylase activity
E	0008654	biological_process	phospholipid biosynthetic process
F	0004609	molecular_function	phosphatidylserine decarboxylase activity
F	0008654	biological_process	phospholipid biosynthetic process
G	0004609	molecular_function	phosphatidylserine decarboxylase activity
G	0008654	biological_process	phospholipid biosynthetic process
H	0004609	molecular_function	phosphatidylserine decarboxylase activity
H	0008654	biological_process	phospholipid biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	12
Details	binding site for residues 9TL I 301 and PPI I 254

Chain	Residue
A	TYR45
A	VAL206
A	PHE250
I	THR255
A	TYR137
A	LEU138
A	SER166
A	VAL167
A	VAL201
A	ALA203
A	THR204
A	ILE205

---

site_id	AC2
Number of Residues	10
Details	binding site for Di-peptide PPI J 254 and THR J 255

Chain	Residue
B	THR136
B	TYR137
B	LEU138
B	VAL167
B	PHE179
B	LEU200
B	VAL201
B	PHE250
J	VAL256
J	PEE301

---

site_id	AC3
Number of Residues	12
Details	binding site for residues 9TL J 301 and PPI J 254

Chain	Residue
B	LEU13
B	TYR45
B	TYR137
B	LEU138
B	SER166
B	VAL167
B	ASN168
B	ALA203
B	THR204
B	ILE205
B	PHE250
J	THR255

---

site_id	AC4
Number of Residues	10
Details	binding site for Di-peptide PPI K 254 and THR K 255

Chain	Residue
C	THR135
C	THR136
C	TYR137
C	LEU138
C	VAL167
C	PHE179
C	VAL201
C	PHE250
K	VAL256
K	PEE301

---

site_id	AC5
Number of Residues	13
Details	binding site for residues 9TL K 301 and PPI K 254

Chain	Residue
C	PHE41
C	TYR45
C	TYR137
C	LEU138
C	PRO140
C	SER166
C	VAL167
C	ASN168
C	ALA203
C	THR204
C	ILE205
C	PHE250
K	THR255

---

site_id	AC6
Number of Residues	11
Details	binding site for Di-peptide PPI L 254 and THR L 255

Chain	Residue
E	THR136
E	TYR137
E	LEU138
E	VAL167
E	PHE179
E	VAL201
E	GLY202
E	ALA203
E	PHE250
L	VAL256
L	PEE301

---

site_id	AC7
Number of Residues	14
Details	binding site for residues 9TL L 301 and PPI L 254

Chain	Residue
E	TYR45
E	TYR137
E	LEU138
E	PRO140
E	SER166
E	VAL167
E	ASN168
E	VAL201
E	GLY202
E	ALA203
E	THR204
E	ILE205
E	PHE250
L	THR255

---

site_id	AC8
Number of Residues	10
Details	binding site for Di-peptide PPI M 254 and THR M 255

Chain	Residue
G	THR136
G	TYR137
G	LEU138
G	VAL167
G	PHE179
G	VAL201
G	VAL206
G	PHE250
M	VAL256
M	PEE301

---

site_id	AC9
Number of Residues	14
Details	binding site for residues 9TL M 301 and PPI M 254

Chain	Residue
G	VAL201
G	ALA203
G	THR204
G	ILE205
G	VAL206
G	PHE250
M	THR255
G	TYR45
G	TYR137
G	LEU138
G	PRO140
G	SER166
G	VAL167
G	ASN168

---

site_id	AD1
Number of Residues	7
Details	binding site for Di-peptide PYR N 254 and THR N 255

Chain	Residue
D	THR136
D	TYR137
D	LEU138
D	VAL167
D	PHE179
D	VAL201
N	VAL256

---

site_id	AD2
Number of Residues	8
Details	binding site for Di-peptide PYR O 254 and THR O 255

Chain	Residue
F	THR136
F	TYR137
F	LEU138
F	VAL167
F	PHE179
F	VAL201
F	ALA203
O	VAL256

---

site_id	AD3
Number of Residues	9
Details	binding site for Di-peptide PYR P 254 and THR P 255

Chain	Residue
H	THR136
H	TYR137
H	LEU138
H	HIS144
H	VAL167
H	PHE179
H	VAL201
H	PHE250
P	VAL256

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	16
Details	Active site: {"description":"Charge relay system; for autoendoproteolytic cleavage activity","evidences":[{"source":"UniProtKB","id":"B3L2V1","evidenceCode":"ECO:0000250"},{"source":"HAMAP-Rule","id":"MF_00662","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	8
Details	Modified residue: {"description":"N-formylmethionine","evidences":[{"source":"PubMed","id":"3042771","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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