3JQE

Crystal structure of pteridine reductase 1 (PTR1) from Trypanosoma brucei in ternary complex with cofactor (NADP+) and inhibitor 2-amino-6-(4-methoxyphenyl)-4-oxo-4,7-dihydro-3H-pyrrolo[2,3-d]pyrimidine-5-carbonitrile (DX8)

Replaces:  3BMK

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0016491	molecular_function	oxidoreductase activity
B	0016491	molecular_function	oxidoreductase activity
C	0016491	molecular_function	oxidoreductase activity
D	0016491	molecular_function	oxidoreductase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	35
Details	BINDING SITE FOR RESIDUE NAP A 269

Chain	Residue
A	ARG14
A	LEU63
A	THR64
A	ASN93
A	ALA94
A	SER95
A	THR126
A	LEU159
A	CYS160
A	TYR174
A	LYS178
A	ILE15
A	PRO204
A	GLY205
A	VAL206
A	SER207
A	LEU208
A	DX8270
A	HOH277
A	HOH288
A	HOH320
A	HOH323
A	HIS33
A	HOH325
A	HOH336
A	HOH344
A	HOH366
A	HOH390
A	HOH401
A	TYR34
A	HIS35
A	ASN36
A	SER37
A	ALA61
A	ASP62

---

site_id	AC2
Number of Residues	13
Details	BINDING SITE FOR RESIDUE DX8 A 270

Chain	Residue
A	ARG14
A	SER95
A	PHE97
A	ASP161
A	MET163
A	CYS168
A	TYR174
A	GLY205
A	PRO210
A	NAP269
A	HOH321
A	HOH326
A	HOH336

---

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ACT A 271

Chain	Residue
A	LYS13
A	ARG14
A	ARG17
A	HOH407
A	HOH427

---

site_id	AC4
Number of Residues	37
Details	BINDING SITE FOR RESIDUE NAP B 269

Chain	Residue
B	ARG14
B	ILE15
B	HIS33
B	TYR34
B	HIS35
B	ASN36
B	SER37
B	ALA61
B	ASP62
B	LEU63
B	THR64
B	ASN93
B	ALA94
B	SER95
B	THR126
B	LEU159
B	CYS160
B	TYR174
B	LYS178
B	PRO204
B	GLY205
B	VAL206
B	SER207
B	LEU208
B	DX8270
B	HOH272
B	HOH279
B	HOH291
B	HOH311
B	HOH337
B	HOH355
B	HOH375
B	HOH411
B	HOH420
B	HOH426
B	HOH459
B	HOH476

---

site_id	AC5
Number of Residues	14
Details	BINDING SITE FOR RESIDUE DX8 B 270

Chain	Residue
B	NAP269
B	HOH305
B	HOH381
B	HOH426
B	HOH457
B	ARG14
B	SER95
B	PHE97
B	ASP161
B	MET163
B	GLN166
B	CYS168
B	TYR174
B	PRO210

---

site_id	AC6
Number of Residues	33
Details	BINDING SITE FOR RESIDUE NAP C 269

Chain	Residue
C	ARG14
C	ILE15
C	TYR34
C	HIS35
C	ASN36
C	SER37
C	ALA61
C	ASP62
C	LEU63
C	THR64
C	ASN93
C	ALA94
C	SER95
C	THR126
C	LEU159
C	CYS160
C	TYR174
C	LYS178
C	PRO204
C	GLY205
C	VAL206
C	SER207
C	LEU208
C	DX8270
C	HOH279
C	HOH280
C	HOH301
C	HOH313
C	HOH329
C	HOH334
C	HOH360
C	HOH386
C	HOH396

---

site_id	AC7
Number of Residues	16
Details	BINDING SITE FOR RESIDUE DX8 C 270

Chain	Residue
C	ARG14
C	SER95
C	PHE97
C	ASP161
C	MET163
C	CYS168
C	TYR174
C	GLY205
C	PRO210
C	TRP221
C	NAP269
C	HOH373
C	HOH388
C	HOH396
C	HOH427
C	HOH490

---

site_id	AC8
Number of Residues	33
Details	BINDING SITE FOR RESIDUE NAP D 269

Chain	Residue
D	ARG14
D	ILE15
D	TYR34
D	HIS35
D	ASN36
D	SER37
D	ALA61
D	ASP62
D	LEU63
D	THR64
D	ASN93
D	ALA94
D	SER95
D	THR126
D	LEU159
D	CYS160
D	TYR174
D	LYS178
D	PRO204
D	GLY205
D	VAL206
D	SER207
D	LEU208
D	DX8270
D	HOH273
D	HOH277
D	HOH311
D	HOH317
D	HOH320
D	HOH333
D	HOH366
D	HOH384
D	HOH421

---

site_id	AC9
Number of Residues	14
Details	BINDING SITE FOR RESIDUE DX8 D 270

Chain	Residue
D	ARG14
D	SER95
D	PHE97
D	ASP161
D	MET163
D	GLN166
D	CYS168
D	TYR174
D	PRO210
D	TRP221
D	NAP269
D	HOH333
D	HOH337
D	HOH363

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ASP161-ALA189

---