Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3H4V

Selective screening and design to identify inhibitors of leishmania major pteridine reductase 1

Replaces: 2P8K

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004155	molecular_function	6,7-dihydropteridine reductase activity
A	0005829	cellular_component	cytosol
A	0006729	biological_process	tetrahydrobiopterin biosynthetic process
A	0016491	molecular_function	oxidoreductase activity
A	0031427	biological_process	response to methotrexate
A	0047040	molecular_function	pteridine reductase activity
B	0004155	molecular_function	6,7-dihydropteridine reductase activity
B	0005829	cellular_component	cytosol
B	0006729	biological_process	tetrahydrobiopterin biosynthetic process
B	0016491	molecular_function	oxidoreductase activity
B	0031427	biological_process	response to methotrexate
B	0047040	molecular_function	pteridine reductase activity
C	0004155	molecular_function	6,7-dihydropteridine reductase activity
C	0005829	cellular_component	cytosol
C	0006729	biological_process	tetrahydrobiopterin biosynthetic process
C	0016491	molecular_function	oxidoreductase activity
C	0031427	biological_process	response to methotrexate
C	0047040	molecular_function	pteridine reductase activity
D	0004155	molecular_function	6,7-dihydropteridine reductase activity
D	0005829	cellular_component	cytosol
D	0006729	biological_process	tetrahydrobiopterin biosynthetic process
D	0016491	molecular_function	oxidoreductase activity
D	0031427	biological_process	response to methotrexate
D	0047040	molecular_function	pteridine reductase activity
E	0004155	molecular_function	6,7-dihydropteridine reductase activity
E	0005829	cellular_component	cytosol
E	0006729	biological_process	tetrahydrobiopterin biosynthetic process
E	0016491	molecular_function	oxidoreductase activity
E	0031427	biological_process	response to methotrexate
E	0047040	molecular_function	pteridine reductase activity
F	0004155	molecular_function	6,7-dihydropteridine reductase activity
F	0005829	cellular_component	cytosol
F	0006729	biological_process	tetrahydrobiopterin biosynthetic process
F	0016491	molecular_function	oxidoreductase activity
F	0031427	biological_process	response to methotrexate
F	0047040	molecular_function	pteridine reductase activity
G	0004155	molecular_function	6,7-dihydropteridine reductase activity
G	0005829	cellular_component	cytosol
G	0006729	biological_process	tetrahydrobiopterin biosynthetic process
G	0016491	molecular_function	oxidoreductase activity
G	0031427	biological_process	response to methotrexate
G	0047040	molecular_function	pteridine reductase activity
H	0004155	molecular_function	6,7-dihydropteridine reductase activity
H	0005829	cellular_component	cytosol
H	0006729	biological_process	tetrahydrobiopterin biosynthetic process
H	0016491	molecular_function	oxidoreductase activity
H	0031427	biological_process	response to methotrexate
H	0047040	molecular_function	pteridine reductase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	35
Details	BINDING SITE FOR RESIDUE NAP A 300

Chain	Residue
A	ARG17
A	LEU66
A	SER67
A	ASN109
A	ALA110
A	SER111
A	SER112
A	ASP142
A	MET179
A	VAL180
A	TYR194
A	LEU18
A	LYS198
A	PRO224
A	GLY225
A	LEU226
A	SER227
A	HOH290
A	HOH293
A	HOH295
A	DVP301
A	HOH346
A	HIS36
A	HOH348
A	HOH366
A	HOH401
A	HOH880
A	HOH886
A	HOH1097
A	TYR37
A	HIS38
A	ARG39
A	SER40
A	ALA64
A	ASP65

site_id	AC2
Number of Residues	13
Details	BINDING SITE FOR RESIDUE DVP A 301

Chain	Residue
A	ARG17
A	SER111
A	PHE113
A	LEU188
A	TYR194
A	MET233
A	NAP300
A	HOH352
A	HOH938
A	HOH1000
A	HOH1049
A	HOH1069
A	HOH1097

site_id	AC3
Number of Residues	29
Details	BINDING SITE FOR RESIDUE NAP B 300

Chain	Residue
B	ARG17
B	LEU18
B	HIS36
B	TYR37
B	HIS38
B	ARG39
B	SER40
B	ALA64
B	ASP65
B	LEU66
B	SER67
B	ASN109
B	ALA110
B	SER111
B	SER112
B	ASP142
B	MET179
B	VAL180
B	LYS198
B	PRO224
B	GLY225
B	SER227
B	DVP301
B	HOH305
B	HOH334
B	HOH349
B	HOH357
B	HOH908
B	HOH1034

site_id	AC4
Number of Residues	10
Details	BINDING SITE FOR RESIDUE DVP B 301

Chain	Residue
B	ARG17
B	SER111
B	PHE113
B	TYR191
B	TYR194
B	LEU226
B	NAP300
B	HOH845
B	HOH1043
C	HOH957

site_id	AC5
Number of Residues	30
Details	BINDING SITE FOR RESIDUE NAP C 300

Chain	Residue
C	ALA110
C	SER111
C	SER112
C	ASP142
C	VAL180
C	ASP181
C	TYR194
C	LYS198
C	PRO224
C	GLY225
C	LEU226
C	SER227
C	DVP301
C	HOH313
C	HOH327
C	HOH334
C	HOH345
C	HOH392
C	ARG17
C	LEU18
C	HIS36
C	TYR37
C	HIS38
C	ARG39
C	SER40
C	ALA64
C	ASP65
C	LEU66
C	SER67
C	ASN109

site_id	AC6
Number of Residues	9
Details	BINDING SITE FOR RESIDUE DVP C 301

Chain	Residue
C	ARG17
C	SER111
C	PHE113
C	LEU188
C	TYR191
C	TYR194
C	HIS241
C	NAP300
C	HOH351

site_id	AC7
Number of Residues	30
Details	BINDING SITE FOR RESIDUE NAP D 300

Chain	Residue
D	ARG17
D	LEU18
D	HIS36
D	TYR37
D	HIS38
D	ARG39
D	SER40
D	ALA64
D	ASP65
D	LEU66
D	SER67
D	ASN109
D	ALA110
D	SER111
D	SER112
D	ASP142
D	MET179
D	VAL180
D	ASP181
D	TYR194
D	LYS198
D	PRO224
D	GLY225
D	LEU226
D	SER227
D	HOH291
D	DVP301
D	HOH332
D	HOH374
D	HOH414

site_id	AC8
Number of Residues	11
Details	BINDING SITE FOR RESIDUE DVP D 301

Chain	Residue
D	ARG17
D	SER111
D	PHE113
D	ASP181
D	LEU188
D	TYR191
D	TYR194
D	HIS241
D	NAP300
D	HOH306
D	HOH1008

site_id	AC9
Number of Residues	31
Details	BINDING SITE FOR RESIDUE NAP E 300

Chain	Residue
E	LYS16
E	ARG17
E	LEU18
E	HIS36
E	TYR37
E	HIS38
E	ARG39
E	SER40
E	ALA64
E	ASP65
E	LEU66
E	SER67
E	ASN109
E	ALA110
E	SER111
E	SER112
E	ASP142
E	MET179
E	VAL180
E	LYS198
E	PRO224
E	GLY225
E	SER227
E	DVP301
E	HOH503
E	HOH505
E	HOH537
E	HOH558
E	HOH564
E	HOH657
E	HOH978

site_id	BC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE DVP E 301

Chain	Residue
E	ARG17
E	SER111
E	PHE113
E	TYR191
E	TYR194
E	NAP300

site_id	BC2
Number of Residues	32
Details	BINDING SITE FOR RESIDUE NAP F 300

Chain	Residue
F	ARG17
F	LEU18
F	HIS36
F	TYR37
F	HIS38
F	ARG39
F	SER40
F	ALA64
F	ASP65
F	LEU66
F	SER67
F	ASN109
F	ALA110
F	SER111
F	SER112
F	ASP142
F	MET179
F	VAL180
F	ASP181
F	TYR194
F	LYS198
F	PRO224
F	GLY225
F	LEU226
F	SER227
F	DVP301
F	HOH526
F	HOH539
F	HOH557
F	HOH559
F	HOH581
F	HOH622

site_id	BC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE DVP F 301

Chain	Residue
F	ARG17
F	SER111
F	PHE113
F	LEU188
F	TYR194
F	MET233
F	NAP300
F	HOH549

site_id	BC4
Number of Residues	26
Details	BINDING SITE FOR RESIDUE NAP G 300

Chain	Residue
G	ARG17
G	LEU18
G	HIS36
G	TYR37
G	HIS38
G	ARG39
G	SER40
G	ALA64
G	ASP65
G	LEU66
G	SER67
G	ASN109
G	SER111
G	ASP142
G	MET179
G	VAL180
G	ASP181
G	LYS198
G	SER227
G	DVP301
G	HOH692
G	HOH722
G	HOH742
G	HOH746
G	HOH747
G	HOH778

site_id	BC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE DVP G 301

Chain	Residue
G	ARG17
G	SER111
G	PHE113
G	LEU188
G	TYR194
G	GLY225
G	LEU226
G	NAP300

site_id	BC6
Number of Residues	30
Details	BINDING SITE FOR RESIDUE NAP H 300

Chain	Residue
H	LYS16
H	ARG17
H	LEU18
H	HIS36
H	TYR37
H	HIS38
H	ARG39
H	SER40
H	LEU66
H	SER67
H	ASN109
H	SER111
H	SER112
H	ASP142
H	SER146
H	VAL180
H	ASP181
H	TYR194
H	LYS198
H	PRO224
H	GLY225
H	LEU226
H	SER227
H	DVP301
H	HOH730
H	HOH740
H	HOH743
H	HOH768
H	HOH795
H	HOH800

site_id	BC7
Number of Residues	11
Details	BINDING SITE FOR RESIDUE DVP H 301

Chain	Residue
H	ARG17
H	SER111
H	PHE113
H	ASP181
H	LEU188
H	TYR191
H	TYR194
H	GLY225
H	ASP232
H	HIS241
H	NAP300

Functional Information from PROSITE/UniProt

site_id	PS00061
Number of Residues	29
Details	ADH_SHORT Short-chain dehydrogenases/reductases family signature. DamtnqpllgYtiYTMAKGALeGLTrSAA

Chain	Residue	Details
A	ASP181-ALA209

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	Active site: {"description":"Proton acceptor"}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	184
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"11373620","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1qsg

Chain	Residue	Details
A	LYS198
A	TYR191

site_id	CSA10
Number of Residues	2
Details	Annotated By Reference To The Literature 1qsg

Chain	Residue	Details
B	LYS198
B	TYR194

site_id	CSA11
Number of Residues	2
Details	Annotated By Reference To The Literature 1qsg

Chain	Residue	Details
C	LYS198
C	TYR194

site_id	CSA12
Number of Residues	2
Details	Annotated By Reference To The Literature 1qsg

Chain	Residue	Details
D	LYS198
D	TYR194

site_id	CSA13
Number of Residues	2
Details	Annotated By Reference To The Literature 1qsg

Chain	Residue	Details
E	LYS198
E	TYR194

site_id	CSA14
Number of Residues	2
Details	Annotated By Reference To The Literature 1qsg

Chain	Residue	Details
F	LYS198
F	TYR194

site_id	CSA15
Number of Residues	2
Details	Annotated By Reference To The Literature 1qsg

Chain	Residue	Details
G	LYS198
G	TYR194

site_id	CSA16
Number of Residues	2
Details	Annotated By Reference To The Literature 1qsg

Chain	Residue	Details
H	LYS198
H	TYR194

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1qsg

Chain	Residue	Details
B	LYS198
B	TYR191

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1qsg

Chain	Residue	Details
C	LYS198
C	TYR191

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1qsg

Chain	Residue	Details
D	LYS198
D	TYR191

site_id	CSA5
Number of Residues	2
Details	Annotated By Reference To The Literature 1qsg

Chain	Residue	Details
E	LYS198
E	TYR191

site_id	CSA6
Number of Residues	2
Details	Annotated By Reference To The Literature 1qsg

Chain	Residue	Details
F	LYS198
F	TYR191

site_id	CSA7
Number of Residues	2
Details	Annotated By Reference To The Literature 1qsg

Chain	Residue	Details
G	LYS198
G	TYR191

site_id	CSA8
Number of Residues	2
Details	Annotated By Reference To The Literature 1qsg

Chain	Residue	Details
H	LYS198
H	TYR191

site_id	CSA9
Number of Residues	2
Details	Annotated By Reference To The Literature 1qsg

Chain	Residue	Details
A	LYS198
A	TYR194

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