Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

7KM3

Dodecameric Structure of the Chlamydia trachomatis Flavin Prenyltransferase UbiX Ortholog CT220 with FMN and DMAP

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004659	molecular_function	prenyltransferase activity
A	0016740	molecular_function	transferase activity
A	0016831	molecular_function	carboxy-lyase activity
A	0106141	molecular_function	flavin prenyltransferase activity
B	0003824	molecular_function	catalytic activity
B	0004659	molecular_function	prenyltransferase activity
B	0016740	molecular_function	transferase activity
B	0016831	molecular_function	carboxy-lyase activity
B	0106141	molecular_function	flavin prenyltransferase activity
C	0003824	molecular_function	catalytic activity
C	0004659	molecular_function	prenyltransferase activity
C	0016740	molecular_function	transferase activity
C	0016831	molecular_function	carboxy-lyase activity
C	0106141	molecular_function	flavin prenyltransferase activity
D	0003824	molecular_function	catalytic activity
D	0004659	molecular_function	prenyltransferase activity
D	0016740	molecular_function	transferase activity
D	0016831	molecular_function	carboxy-lyase activity
D	0106141	molecular_function	flavin prenyltransferase activity
E	0003824	molecular_function	catalytic activity
E	0004659	molecular_function	prenyltransferase activity
E	0016740	molecular_function	transferase activity
E	0016831	molecular_function	carboxy-lyase activity
E	0106141	molecular_function	flavin prenyltransferase activity
F	0003824	molecular_function	catalytic activity
F	0004659	molecular_function	prenyltransferase activity
F	0016740	molecular_function	transferase activity
F	0016831	molecular_function	carboxy-lyase activity
F	0106141	molecular_function	flavin prenyltransferase activity
G	0003824	molecular_function	catalytic activity
G	0004659	molecular_function	prenyltransferase activity
G	0016740	molecular_function	transferase activity
G	0016831	molecular_function	carboxy-lyase activity
G	0106141	molecular_function	flavin prenyltransferase activity
H	0003824	molecular_function	catalytic activity
H	0004659	molecular_function	prenyltransferase activity
H	0016740	molecular_function	transferase activity
H	0016831	molecular_function	carboxy-lyase activity
H	0106141	molecular_function	flavin prenyltransferase activity
I	0003824	molecular_function	catalytic activity
I	0004659	molecular_function	prenyltransferase activity
I	0016740	molecular_function	transferase activity
I	0016831	molecular_function	carboxy-lyase activity
I	0106141	molecular_function	flavin prenyltransferase activity
J	0003824	molecular_function	catalytic activity
J	0004659	molecular_function	prenyltransferase activity
J	0016740	molecular_function	transferase activity
J	0016831	molecular_function	carboxy-lyase activity
J	0106141	molecular_function	flavin prenyltransferase activity
K	0003824	molecular_function	catalytic activity
K	0004659	molecular_function	prenyltransferase activity
K	0016740	molecular_function	transferase activity
K	0016831	molecular_function	carboxy-lyase activity
K	0106141	molecular_function	flavin prenyltransferase activity
L	0003824	molecular_function	catalytic activity
L	0004659	molecular_function	prenyltransferase activity
L	0016740	molecular_function	transferase activity
L	0016831	molecular_function	carboxy-lyase activity
L	0106141	molecular_function	flavin prenyltransferase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	18
Details	binding site for residue FMN L 301

Chain	Residue
D	ILE72
L	SER36
L	SER38
L	THR42
L	SER92
L	VAL93
L	THR95
L	ARG127
L	GLU128
L	HOH423
D	GLU73
D	ALA104
D	ASP105
D	4LR302
L	SER9
L	GLY10
L	ALA11
L	SER12

site_id	AC2
Number of Residues	19
Details	binding site for residue FMN I 301

Chain	Residue
B	4LR302
I	SER9
I	GLY10
I	ALA11
I	SER12
I	SER36
I	SER38
I	THR42
I	TYR45
I	SER92
I	VAL93
I	ALA94
I	THR95
I	ARG127
I	GLU128
L	ILE72
L	ALA104
L	ASP105
L	ARG110

site_id	AC3
Number of Residues	3
Details	binding site for residue 4LR I 302

Chain	Residue
D	GLU128
D	FMN301
I	LYS117

site_id	AC4
Number of Residues	20
Details	binding site for residue FMN A 301

Chain	Residue
A	SER9
A	GLY10
A	ALA11
A	SER12
A	SER36
A	SER38
A	SER92
A	VAL93
A	THR95
A	ARG127
A	GLU128
A	4LR302
A	HOH408
A	HOH420
A	HOH437
A	HOH439
B	ILE72
B	GLU73
B	ALA104
B	ASP105

site_id	AC5
Number of Residues	6
Details	binding site for residue 4LR A 302

Chain	Residue
A	GLU128
A	FMN301
A	HOH403
B	ARG110
B	LYS117
E	TYR157

site_id	AC6
Number of Residues	8
Details	binding site for residue 4LR A 303

Chain	Residue
A	ILE72
A	SER77
A	SER78
A	ARG110
A	LYS117
G	TYR157
K	GLU128
K	FMN301

site_id	AC7
Number of Residues	21
Details	binding site for residue FMN B 301

Chain	Residue
B	SER9
B	GLY10
B	ALA11
B	SER12
B	SER36
B	SER38
B	SER92
B	VAL93
B	THR95
B	ARG127
B	GLU128
B	HOH425
B	HOH435
B	HOH443
B	HOH444
K	ILE72
K	GLU73
K	ALA104
K	ASP105
K	ARG110
K	4LR302

site_id	AC8
Number of Residues	4
Details	binding site for residue 4LR B 302

Chain	Residue
B	TYR157
I	ARG127
I	GLU128
I	FMN301

site_id	AC9
Number of Residues	19
Details	binding site for residue FMN C 301

Chain	Residue
C	SER9
C	GLY10
C	ALA11
C	SER12
C	SER36
C	SER38
C	SER92
C	VAL93
C	THR95
C	ARG127
C	GLU128
C	4LR302
C	HOH424
C	HOH426
E	ILE72
E	GLU73
E	ALA104
E	ASP105
E	ARG110

site_id	AD1
Number of Residues	6
Details	binding site for residue 4LR C 302

Chain	Residue
C	GLU128
C	FMN301
E	ILE72
E	SER78
E	ARG110
E	LYS117

site_id	AD2
Number of Residues	10
Details	binding site for residue 4LR C 303

Chain	Residue
C	ILE72
C	SER77
C	SER78
C	GLY79
C	ARG110
C	LYS117
F	TYR157
F	TRP188
J	GLU128
J	FMN301

site_id	AD3
Number of Residues	16
Details	binding site for residue FMN D 301

Chain	Residue
D	SER9
D	GLY10
D	ALA11
D	SER12
D	SER36
D	SER38
D	TYR45
D	SER92
D	VAL93
D	THR95
D	ARG127
D	GLU128
D	HOH417
I	ALA104
I	ARG110
I	4LR302

site_id	AD4
Number of Residues	10
Details	binding site for residue 4LR D 302

Chain	Residue
C	TYR157
D	ILE72
D	SER77
D	SER78
D	GLY79
D	ARG110
D	LYS117
L	ARG127
L	GLU128
L	FMN301

site_id	AD5
Number of Residues	21
Details	binding site for residue FMN E 301

Chain	Residue
E	SER9
E	GLY10
E	ALA11
E	SER12
E	SER36
E	SER38
E	SER92
E	VAL93
E	THR95
E	ARG127
E	GLU128
E	HOH403
E	HOH408
E	HOH417
E	HOH418
J	ILE72
J	GLU73
J	ALA104
J	ASP105
J	ARG110
J	4LR302

site_id	AD6
Number of Residues	18
Details	binding site for residue FMN F 301

Chain	Residue
F	SER9
F	GLY10
F	ALA11
F	SER12
F	SER36
F	SER38
F	SER92
F	VAL93
F	THR95
F	ARG127
F	GLU128
F	4LR302
F	HOH407
F	HOH431
G	ILE72
G	GLU73
G	ALA104
G	ASP105

site_id	AD7
Number of Residues	8
Details	binding site for residue 4LR F 302

Chain	Residue
F	ARG127
F	GLU128
F	ALA129
F	FMN301
G	SER77
G	ARG110
G	LYS117
J	TYR157

site_id	AD8
Number of Residues	9
Details	binding site for residue 4LR F 303

Chain	Residue
D	TYR157
F	ILE72
F	SER77
F	SER78
F	GLY79
F	ARG110
F	LYS117
H	ARG127
H	GLU128

site_id	AD9
Number of Residues	19
Details	binding site for residue FMN G 301

Chain	Residue
G	SER9
G	GLY10
G	ALA11
G	SER12
G	SER36
G	SER38
G	THR42
G	SER92
G	VAL93
G	THR95
G	ARG127
G	GLU128
G	HOH413
G	HOH417
H	GLU73
H	ALA104
H	ASP105
H	ARG110
K	4LR303

site_id	AE1
Number of Residues	19
Details	binding site for residue FMN H 301

Chain	Residue
F	GLU73
F	ALA104
F	ASP105
F	ARG110
H	SER9
H	GLY10
H	ALA11
H	SER12
H	SER36
H	SER38
H	THR42
H	SER92
H	VAL93
H	THR95
H	ARG127
H	GLU128
H	HOH417
H	HOH428
H	HOH429

site_id	AE2
Number of Residues	20
Details	binding site for residue FMN J 301

Chain	Residue
C	ILE72
C	GLU73
C	ALA104
C	ASP105
C	ARG110
C	4LR303
J	SER9
J	GLY10
J	ALA11
J	SER12
J	SER36
J	SER38
J	SER92
J	VAL93
J	THR95
J	ARG127
J	GLU128
J	HOH411
J	HOH425
J	HOH433

site_id	AE3
Number of Residues	9
Details	binding site for residue 4LR J 302

Chain	Residue
A	TYR157
E	GLU128
E	FMN301
J	ILE72
J	SER78
J	GLY79
J	ARG110
J	LYS117
J	HOH439

site_id	AE4
Number of Residues	19
Details	binding site for residue FMN K 301

Chain	Residue
A	GLU73
A	ALA104
A	ASP105
A	4LR303
K	SER9
K	GLY10
K	ALA11
K	SER12
K	SER36
K	SER38
K	SER92
K	VAL93
K	THR95
K	ARG127
K	GLU128
K	HOH415
K	HOH422
K	HOH423
K	HOH435

site_id	AE5
Number of Residues	11
Details	binding site for residue 4LR K 302

Chain	Residue
B	ARG127
B	GLU128
B	FMN301
I	TYR157
I	HOH409
K	ILE72
K	SER77
K	SER78
K	GLY79
K	ARG110
K	LYS117

site_id	AE6
Number of Residues	6
Details	binding site for residue 4LR K 303

Chain	Residue
G	GLU128
G	FMN301
H	ARG110
H	LYS117
K	TYR157
K	TRP188

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	108
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01984","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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