DRUG BINDING INTERFACES MAPPED TO 'DIHYDROFOLATE REDUCTASE (DHFR)'

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