DRUG BINDING INTERFACES MAPPED TO '3fl9'

List of Binding Interfaces
(Click on the entry ID to view details of interfaces and pattern clusters)
(Note that ASSAM search use only 3-12 residue containing patterns)
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DrReposER ID PDB Ligand Organism Macromolecule Pfam Res. Interface HETATM
3FL9_A_TOPA200 3fl9 TOP

DB00440
(Trimethoprim)
Bacillus
anthracis
DIHYDROFOLATE
REDUCTASE (DHFR)
PF00186
(DHFR_1)
10 MET A   6
ALA A   8
LEU A  21
GLU A  28
VAL A  32
ALA A  50
ILE A  51
LEU A  55
PHE A  96
TYR A 102
TOP A 200
3FL9_B_TOPB200 3fl9 TOP

DB00440
(Trimethoprim)
Bacillus
anthracis
DIHYDROFOLATE
REDUCTASE (DHFR)
no annotation 12 MET B   6
ALA B   8
ASN B  20
LEU B  21
GLU B  28
LEU B  29
VAL B  32
ILE B  51
LEU B  55
PHE B  96
TYR B 102
THR B 115
TOP B 200
3FL9_C_TOPC200 3fl9 TOP

DB00440
(Trimethoprim)
Bacillus
anthracis
DIHYDROFOLATE
REDUCTASE (DHFR)
no annotation 11 MET C   6
ALA C   8
ASN C  20
LEU C  21
GLU C  28
LEU C  29
VAL C  32
ILE C  51
LEU C  55
PHE C  96
THR C 115
TOP C 200
3FL9_D_TOPD200 3fl9 TOP

DB00440
(Trimethoprim)
Bacillus
anthracis
DIHYDROFOLATE
REDUCTASE (DHFR)
no annotation 9 MET D   6
ALA D   8
LEU D  21
GLU D  28
VAL D  32
ILE D  51
LEU D  55
PHE D  96
TYR D 102
TOP D 200
3FL9_E_TOPE200 3fl9 TOP

DB00440
(Trimethoprim)
Bacillus
anthracis
DIHYDROFOLATE
REDUCTASE (DHFR)
no annotation 10 MET E   6
ALA E   8
LEU E  21
GLU E  28
LEU E  29
VAL E  32
ILE E  51
LEU E  55
PHE E  96
THR E 115
TOP E 200
3FL9_F_TOPF200 3fl9 TOP

DB00440
(Trimethoprim)
Bacillus
anthracis
DIHYDROFOLATE
REDUCTASE (DHFR)
no annotation 10 MET F   6
ALA F   8
ASN F  20
LEU F  21
GLU F  28
VAL F  32
ALA F  50
ILE F  51
LEU F  55
PHE F  96
TOP F 200
3FL9_G_TOPG200 3fl9 TOP

DB00440
(Trimethoprim)
Bacillus
anthracis
DIHYDROFOLATE
REDUCTASE (DHFR)
no annotation 12 MET G   6
ALA G   8
ASN G  20
LEU G  21
GLU G  28
LEU G  29
VAL G  32
ILE G  51
LEU G  55
PHE G  96
TYR G 102
THR G 115
TOP G 200
3FL9_H_TOPH200 3fl9 TOP

DB00440
(Trimethoprim)
Bacillus
anthracis
DIHYDROFOLATE
REDUCTASE (DHFR)
no annotation 9 MET H   6
ALA H   8
GLU H  28
LEU H  29
VAL H  32
ILE H  51
LEU H  55
PHE H  96
THR H 115
TOP H 200