2RCY

Crystal structure of Plasmodium falciparum pyrroline carboxylate reductase (MAL13P1.284) with NADP bound

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0004735	molecular_function	pyrroline-5-carboxylate reductase activity
A	0006561	biological_process	obsolete proline biosynthetic process
A	0016491	molecular_function	oxidoreductase activity
A	0055129	biological_process	L-proline biosynthetic process
B	0000166	molecular_function	nucleotide binding
B	0004735	molecular_function	pyrroline-5-carboxylate reductase activity
B	0006561	biological_process	obsolete proline biosynthetic process
B	0016491	molecular_function	oxidoreductase activity
B	0055129	biological_process	L-proline biosynthetic process
C	0000166	molecular_function	nucleotide binding
C	0004735	molecular_function	pyrroline-5-carboxylate reductase activity
C	0006561	biological_process	obsolete proline biosynthetic process
C	0016491	molecular_function	oxidoreductase activity
C	0055129	biological_process	L-proline biosynthetic process
D	0000166	molecular_function	nucleotide binding
D	0004735	molecular_function	pyrroline-5-carboxylate reductase activity
D	0006561	biological_process	obsolete proline biosynthetic process
D	0016491	molecular_function	oxidoreductase activity
D	0055129	biological_process	L-proline biosynthetic process
E	0000166	molecular_function	nucleotide binding
E	0004735	molecular_function	pyrroline-5-carboxylate reductase activity
E	0006561	biological_process	obsolete proline biosynthetic process
E	0016491	molecular_function	oxidoreductase activity
E	0055129	biological_process	L-proline biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG A 263

Chain	Residue
A	LYS203
A	VAL206
E	LYS203

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site_id	AC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG B 263

Chain	Residue
B	LYS203
C	LYS203

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site_id	AC3
Number of Residues	27
Details	BINDING SITE FOR RESIDUE NAP B 264

Chain	Residue
B	TYR37
B	PRO39
B	SER40
B	LYS42
B	ASN52
B	ALA65
B	VAL66
B	PRO68
B	ILE70
B	VAL74
B	ILE90
B	CYS91
B	GLY92
B	MSE113
B	THR116
B	HOH285
B	HOH289
B	HOH316
B	HOH317
B	HOH331
C	ASN222
C	ILE223
C	SER225
B	GLY11
B	GLY13
B	GLN14
B	MSE15

---

site_id	AC4
Number of Residues	27
Details	BINDING SITE FOR RESIDUE NAP A 264

Chain	Residue
A	GLY11
A	GLY13
A	GLN14
A	MSE15
A	PRO39
A	SER40
A	LYS42
A	ASN52
A	ALA65
A	VAL66
A	LYS67
A	PRO68
A	ILE70
A	VAL74
A	ILE90
A	CYS91
A	GLY92
A	MSE113
A	PRO114
A	THR116
A	HOH298
A	HOH313
A	HOH316
A	HOH321
E	ASN222
E	ILE223
E	SER225

---

site_id	AC5
Number of Residues	26
Details	BINDING SITE FOR RESIDUE NAP D 264

Chain	Residue
D	GLY13
D	GLN14
D	MSE15
D	PRO39
D	SER40
D	LYS42
D	ASN52
D	ALA65
D	VAL66
D	LYS67
D	PRO68
D	ILE70
D	ILE90
D	CYS91
D	GLY92
D	MSE113
D	PRO114
D	THR116
D	ASN222
D	ILE223
D	SER225
D	HOH277
D	HOH285
D	HOH289
D	HOH304
D	HOH308

---

site_id	AC6
Number of Residues	29
Details	BINDING SITE FOR RESIDUE NAP E 264

Chain	Residue
E	PRO68
E	ILE70
E	ILE90
E	CYS91
E	GLY92
E	MSE113
E	PRO114
E	THR116
E	HOH286
E	HOH297
E	HOH299
E	HOH306
E	HOH308
E	HOH335
E	HOH337
A	ASN222
A	ILE223
A	SER225
E	GLY11
E	GLY13
E	GLN14
E	MSE15
E	PRO39
E	SER40
E	LYS42
E	ASN52
E	ALA65
E	VAL66
E	LYS67

---

site_id	AC7
Number of Residues	28
Details	BINDING SITE FOR RESIDUE NAP C 264

Chain	Residue
B	ASN222
B	ILE223
B	SER225
C	GLY11
C	GLY13
C	GLN14
C	MSE15
C	PRO39
C	ASN52
C	ALA65
C	VAL66
C	PRO68
C	ILE70
C	VAL74
C	ILE90
C	CYS91
C	GLY92
C	MSE113
C	PRO114
C	THR116
C	HOH270
C	HOH301
C	HOH306
C	HOH309
C	HOH335
C	HOH341
C	HOH345
C	HOH346

---

site_id	AC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL A 265

Chain	Residue
A	MSE208
A	GLN214
A	LEU219
A	ASN222
A	HOH275
E	GLN14
E	THR116

---

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL B 265

Chain	Residue
B	ASN4
B	ILE28
B	TYR140
B	ASP143
B	ILE144

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