Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

7MFO

X-ray structure of the L136 Aminotransferase from Acanthamoeba polyphaga mimivirus in the presence of TDP and PMP

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000271	biological_process	polysaccharide biosynthetic process
A	0019180	molecular_function	dTDP-4-amino-4,6-dideoxygalactose transaminase activity
A	0030170	molecular_function	pyridoxal phosphate binding
B	0000271	biological_process	polysaccharide biosynthetic process
B	0019180	molecular_function	dTDP-4-amino-4,6-dideoxygalactose transaminase activity
B	0030170	molecular_function	pyridoxal phosphate binding
C	0000271	biological_process	polysaccharide biosynthetic process
C	0019180	molecular_function	dTDP-4-amino-4,6-dideoxygalactose transaminase activity
C	0030170	molecular_function	pyridoxal phosphate binding
D	0000271	biological_process	polysaccharide biosynthetic process
D	0019180	molecular_function	dTDP-4-amino-4,6-dideoxygalactose transaminase activity
D	0030170	molecular_function	pyridoxal phosphate binding
E	0000271	biological_process	polysaccharide biosynthetic process
E	0019180	molecular_function	dTDP-4-amino-4,6-dideoxygalactose transaminase activity
E	0030170	molecular_function	pyridoxal phosphate binding
F	0000271	biological_process	polysaccharide biosynthetic process
F	0019180	molecular_function	dTDP-4-amino-4,6-dideoxygalactose transaminase activity
F	0030170	molecular_function	pyridoxal phosphate binding
G	0000271	biological_process	polysaccharide biosynthetic process
G	0019180	molecular_function	dTDP-4-amino-4,6-dideoxygalactose transaminase activity
G	0030170	molecular_function	pyridoxal phosphate binding
H	0000271	biological_process	polysaccharide biosynthetic process
H	0019180	molecular_function	dTDP-4-amino-4,6-dideoxygalactose transaminase activity
H	0030170	molecular_function	pyridoxal phosphate binding
I	0000271	biological_process	polysaccharide biosynthetic process
I	0019180	molecular_function	dTDP-4-amino-4,6-dideoxygalactose transaminase activity
I	0030170	molecular_function	pyridoxal phosphate binding
J	0000271	biological_process	polysaccharide biosynthetic process
J	0019180	molecular_function	dTDP-4-amino-4,6-dideoxygalactose transaminase activity
J	0030170	molecular_function	pyridoxal phosphate binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	16
Details	binding site for residue PMP A 401

Chain	Residue
A	GLY64
A	TYR307
A	HOH549
A	HOH574
A	HOH615
A	HOH639
A	HOH707
B	ASN229
A	THR65
A	PHE92
A	SER94
A	ASP156
A	ALA158
A	SER180
A	HIS182
A	LYS185

site_id	AC2
Number of Residues	4
Details	binding site for residue PO4 A 402

Chain	Residue
A	LYS5
A	PHE301
A	GLU340
A	ILE341

site_id	AC3
Number of Residues	7
Details	binding site for residue EDO A 403

Chain	Residue
A	LYS263
A	LYS278
A	LYS279
A	ASN280
A	HOH614
J	ASN140
J	ASP144

site_id	AC4
Number of Residues	2
Details	binding site for residue CL A 404

Chain	Residue
A	LEU166
A	LYS278

site_id	AC5
Number of Residues	22
Details	binding site for residue TYD B 401

Chain	Residue
A	TRP8
A	VAL9
A	HIS182
A	HIS183
A	THR184
A	TYR306
A	HOH549
B	ASN30
B	GLN31
B	TYR32
B	THR33
B	ASN34
B	HOH510
B	HOH518
B	HOH524
B	HOH543
B	HOH561
B	HOH564
B	HOH581
B	HOH694
B	HOH698
B	HOH739

site_id	AC6
Number of Residues	14
Details	binding site for residue PMP B 402

Chain	Residue
A	ASN229
B	GLY64
B	THR65
B	PHE92
B	SER94
B	ASP156
B	ALA158
B	SER180
B	LYS185
B	TYR307
B	HOH501
B	HOH577
B	HOH582
B	HOH644

site_id	AC7
Number of Residues	18
Details	binding site for residue TYD B 403

Chain	Residue
A	ASN30
A	GLN31
A	TYR32
A	THR33
A	ASN34
A	HOH572
B	VAL9
B	HIS182
B	HIS183
B	THR184
B	ARG304
B	TYR306
B	HOH501
B	HOH502
B	HOH667
B	HOH725
B	HOH742
B	HOH748

site_id	AC8
Number of Residues	7
Details	binding site for residue EDO B 404

Chain	Residue
B	ILE207
B	ASN210
B	LEU213
B	ASN215
B	HOH590
B	HOH607
B	HOH734

site_id	AC9
Number of Residues	3
Details	binding site for residue EDO B 405

Chain	Residue
B	PHE164
B	LYS279
B	HOH740

site_id	AD1
Number of Residues	16
Details	binding site for residue PMP C 401

Chain	Residue
C	ALA158
C	SER180
C	HIS182
C	LYS185
C	TYR307
C	HOH549
C	HOH554
C	HOH604
D	ASN229
D	HOH505
C	ASN63
C	GLY64
C	THR65
C	PHE92
C	SER94
C	ASP156

site_id	AD2
Number of Residues	14
Details	binding site for residue TYD C 402

Chain	Residue
C	ASN30
C	GLN31
C	TYR32
C	THR33
C	ASN34
C	HOH519
C	HOH707
C	HOH736
D	VAL9
D	HIS182
D	HIS183
D	THR184
D	ARG304
D	TYR306

site_id	AD3
Number of Residues	5
Details	binding site for residue EDO C 403

Chain	Residue
C	ASP109
C	LEU114
C	ASP115
C	LEU116
C	LYS141

site_id	AD4
Number of Residues	20
Details	binding site for residue TYD D 401

Chain	Residue
C	TRP8
C	VAL9
C	HIS182
C	HIS183
C	THR184
C	ARG304
C	TYR306
D	ASN30
D	GLN31
D	TYR32
D	THR33
D	ASN34
D	HOH505
D	HOH507
D	HOH510
D	HOH511
D	HOH518
D	HOH521
D	HOH577
D	HOH666

site_id	AD5
Number of Residues	13
Details	binding site for residue PMP D 402

Chain	Residue
C	ASN229
D	ASN63
D	GLY64
D	THR65
D	PHE92
D	SER94
D	ASP156
D	ALA158
D	SER180
D	LYS185
D	TYR307
D	HOH559
D	HOH561

site_id	AD6
Number of Residues	14
Details	binding site for residue PMP E 401

Chain	Residue
E	ASN63
E	GLY64
E	THR65
E	PHE92
E	SER94
E	ASP156
E	ALA158
E	SER180
E	LYS185
E	TYR307
E	HOH504
E	HOH541
E	HOH647
F	ASN229

site_id	AD7
Number of Residues	21
Details	binding site for residue TYD E 402

Chain	Residue
E	TRP8
E	VAL9
E	HIS182
E	HIS183
E	THR184
E	ARG304
E	TYR306
E	HOH502
E	HOH504
E	HOH561
E	HOH588
E	HOH596
E	HOH686
E	HOH740
E	HOH748
F	ASN30
F	GLN31
F	TYR32
F	THR33
F	ASN34
F	HOH518

site_id	AD8
Number of Residues	19
Details	binding site for residue TYD E 403

Chain	Residue
E	ASN30
E	GLN31
E	TYR32
E	THR33
E	ASN34
E	HOH501
E	HOH506
E	HOH510
E	HOH516
E	HOH626
E	HOH689
E	HOH742
E	HOH773
F	VAL9
F	HIS182
F	HIS183
F	THR184
F	ARG304
F	TYR306

site_id	AD9
Number of Residues	4
Details	binding site for residue EDO E 404

Chain	Residue
E	HOH515
E	HOH546
E	HOH580
E	HOH623

site_id	AE1
Number of Residues	15
Details	binding site for residue PMP F 401

Chain	Residue
E	ASN229
F	ASN63
F	GLY64
F	THR65
F	PHE92
F	SER94
F	ASP156
F	ALA158
F	SER180
F	LYS185
F	TYR307
F	HOH548
F	HOH581
F	HOH586
F	HOH596

site_id	AE2
Number of Residues	5
Details	binding site for residue EDO F 402

Chain	Residue
F	ASP109
F	LEU114
F	ASP115
F	LEU116
F	LYS141

site_id	AE3
Number of Residues	14
Details	binding site for residue PMP G 401

Chain	Residue
G	ASN63
G	GLY64
G	THR65
G	PHE92
G	SER94
G	ASP156
G	ALA158
G	SER180
G	LYS185
G	TYR307
G	HOH535
G	HOH572
H	ASN229
H	HOH506

site_id	AE4
Number of Residues	12
Details	binding site for residue TYD G 402

Chain	Residue
G	ASN30
G	GLN31
G	TYR32
G	THR33
G	ASN34
G	HOH526
H	VAL9
H	HIS183
H	THR184
H	ARG304
H	TYR306
H	HOH673

site_id	AE5
Number of Residues	20
Details	binding site for residue TYD H 401

Chain	Residue
G	TRP8
G	VAL9
G	HIS182
G	HIS183
G	THR184
G	ARG304
G	TYR306
H	ASN30
H	GLN31
H	TYR32
H	THR33
H	ASN34
H	HOH502
H	HOH503
H	HOH506
H	HOH510
H	HOH514
H	HOH623
H	HOH626
H	HOH638

site_id	AE6
Number of Residues	13
Details	binding site for residue PMP H 402

Chain	Residue
G	ASN229
H	GLY64
H	THR65
H	PHE92
H	SER94
H	ASP156
H	ALA158
H	SER180
H	HIS182
H	LYS185
H	TYR307
H	HOH595
H	HOH604

site_id	AE7
Number of Residues	14
Details	binding site for residue PMP I 401

Chain	Residue
I	ASN63
I	GLY64
I	THR65
I	THR91
I	PHE92
I	SER94
I	ASP156
I	ALA158
I	SER180
I	LYS185
I	TYR307
I	HOH546
I	HOH548
J	ASN229

site_id	AE8
Number of Residues	17
Details	binding site for residue TYD I 402

Chain	Residue
I	ASN30
I	GLN31
I	TYR32
I	THR33
I	ASN34
I	HOH502
I	HOH518
I	HOH553
I	HOH581
I	HOH604
J	TRP8
J	VAL9
J	HIS182
J	HIS183
J	THR184
J	ARG304
J	TYR306

site_id	AE9
Number of Residues	17
Details	binding site for residue TYD J 401

Chain	Residue
I	TRP8
I	HIS183
I	THR184
I	ARG304
I	TYR306
I	HOH627
J	ASN30
J	GLN31
J	TYR32
J	THR33
J	ASN34
J	HOH501
J	HOH506
J	HOH544
J	HOH573
J	HOH655
J	HOH690

site_id	AF1
Number of Residues	14
Details	binding site for residue PMP J 402

Chain	Residue
I	ASN229
J	GLY64
J	THR65
J	PHE92
J	SER94
J	ASP156
J	ALA158
J	SER180
J	HIS182
J	LYS185
J	TYR307
J	HOH518
J	HOH559
J	HOH579

site_id	AF2
Number of Residues	4
Details	binding site for residue EDO J 403

Chain	Residue
J	ARG199
J	HOH637
J	HOH646
J	HOH672

site_id	AF3
Number of Residues	5
Details	binding site for residue EDO J 404

Chain	Residue
J	ASP109
J	ASP115
J	LEU116
J	LYS141
J	HOH624

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