3JQQ

Crystal structure of the H286K mutant of Ferredoxin-NADP+ reductase from Plasmodium falciparum in complex with 2'P-AMP

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
E	0016491	molecular_function	oxidoreductase activity
F	0016491	molecular_function	oxidoreductase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	24
Details	BINDING SITE FOR RESIDUE FAD A 415

Chain	Residue
A	ARG101
A	GLY136
A	TYR137
A	CYS138
A	SER139
A	THR180
A	TYR316
A	HOH320
A	HOH325
A	HOH335
A	HOH365
A	LEU102
A	HOH383
A	HOH470
B	LEU102
B	HOH410
B	FAD415
A	TYR103
A	SER104
A	ALA117
A	ILE118
A	LYS119
A	HIS121
A	TYR123

---

site_id	AC2
Number of Residues	21
Details	BINDING SITE FOR RESIDUE A2P A 416

Chain	Residue
A	LYS119
A	THR178
A	GLY216
A	VAL217
A	TYR218
A	SER247
A	TYR258
A	GLN260
A	LYS286
A	SER288
A	HOH318
A	HOH386
A	HOH442
A	HOH570
A	HOH670
A	HOH673
A	HOH1118
B	TYR258
B	LYS287
B	SER288
B	A2P416

---

site_id	AC3
Number of Residues	27
Details	BINDING SITE FOR RESIDUE FAD B 415

Chain	Residue
A	LEU102
A	LYS287
A	HOH376
A	FAD415
B	ARG101
B	LEU102
B	TYR103
B	SER104
B	ALA117
B	ILE118
B	LYS119
B	HIS121
B	TYR123
B	GLY136
B	TYR137
B	CYS138
B	SER139
B	THR180
B	TYR316
B	HOH342
B	HOH372
B	HOH556
B	HOH557
B	HOH569
B	HOH690
B	HOH1085
B	HOH1152

---

site_id	AC4
Number of Residues	22
Details	BINDING SITE FOR RESIDUE A2P B 416

Chain	Residue
A	TYR258
A	SER288
A	A2P416
B	LYS119
B	THR178
B	GLY179
B	GLY216
B	VAL217
B	TYR218
B	SER247
B	TYR258
B	GLN260
B	LYS286
B	SER288
B	HOH322
B	HOH330
B	HOH337
B	HOH354
B	HOH430
B	HOH508
B	HOH710
B	HOH1214

---

site_id	AC5
Number of Residues	25
Details	BINDING SITE FOR RESIDUE FAD C 415

Chain	Residue
C	ILE118
C	LYS119
C	HIS121
C	TYR123
C	GLY136
C	TYR137
C	CYS138
C	SER139
C	THR180
C	TYR316
C	HOH321
C	HOH329
C	HOH332
C	HOH362
C	HOH368
C	HOH392
C	HOH553
C	HOH706
D	LEU102
D	FAD415
C	ARG101
C	LEU102
C	TYR103
C	SER104
C	ALA117

---

site_id	AC6
Number of Residues	20
Details	BINDING SITE FOR RESIDUE A2P C 416

Chain	Residue
C	LYS119
C	GLY216
C	VAL217
C	TYR218
C	SER247
C	TYR258
C	GLN260
C	LYS286
C	SER288
C	HOH325
C	HOH330
C	HOH367
C	HOH393
C	HOH395
C	HOH478
C	HOH562
C	HOH1250
D	TYR258
D	SER288
D	A2P416

---

site_id	AC7
Number of Residues	27
Details	BINDING SITE FOR RESIDUE FAD D 415

Chain	Residue
C	LEU102
C	HOH411
C	FAD415
D	ARG101
D	LEU102
D	TYR103
D	SER104
D	ALA117
D	ILE118
D	LYS119
D	HIS121
D	TYR123
D	GLY136
D	TYR137
D	CYS138
D	SER139
D	THR180
D	TYR316
D	HOH317
D	HOH321
D	HOH342
D	HOH357
D	HOH406
D	HOH661
D	HOH820
D	HOH1076
D	HOH1342

---

site_id	AC8
Number of Residues	21
Details	BINDING SITE FOR RESIDUE A2P D 416

Chain	Residue
C	TYR258
C	LYS287
C	SER288
C	A2P416
D	LYS119
D	THR178
D	GLY179
D	GLY216
D	VAL217
D	TYR218
D	SER247
D	TYR258
D	GLN260
D	LYS286
D	HOH318
D	HOH330
D	HOH335
D	HOH362
D	HOH591
D	HOH666
D	HOH683

---

site_id	AC9
Number of Residues	22
Details	BINDING SITE FOR RESIDUE FAD E 415

Chain	Residue
E	ARG101
E	LEU102
E	TYR103
E	SER104
E	ALA117
E	ILE118
E	LYS119
E	HIS121
E	TYR123
E	GLY136
E	TYR137
E	CYS138
E	SER139
E	THR180
E	TYR316
E	HOH317
E	HOH337
E	HOH524
E	HOH699
F	LEU102
F	FAD415
F	HOH588

---

site_id	BC1
Number of Residues	16
Details	BINDING SITE FOR RESIDUE A2P E 416

Chain	Residue
E	LYS119
E	GLY216
E	VAL217
E	TYR218
E	SER247
E	TYR258
E	GLN260
E	LYS286
E	SER288
E	HOH332
E	HOH509
E	HOH956
F	TYR258
F	LYS287
F	SER288
F	A2P416

---

site_id	BC2
Number of Residues	24
Details	BINDING SITE FOR RESIDUE FAD F 415

Chain	Residue
E	LEU102
E	FAD415
E	HOH431
F	ARG101
F	LEU102
F	TYR103
F	SER104
F	ALA117
F	ILE118
F	LYS119
F	HIS121
F	TYR123
F	GLY136
F	TYR137
F	CYS138
F	SER139
F	THR180
F	TYR316
F	HOH325
F	HOH461
F	HOH560
F	HOH689
F	HOH746
F	HOH916

---

site_id	BC3
Number of Residues	18
Details	BINDING SITE FOR RESIDUE A2P F 416

Chain	Residue
E	TYR258
E	SER288
E	A2P416
F	LYS119
F	THR178
F	GLY179
F	GLY216
F	VAL217
F	TYR218
F	SER247
F	TYR258
F	LYS286
F	SER288
F	ILE289
F	HOH320
F	HOH332
F	HOH567
F	HOH600

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269|PubMed:17258767, ECO:0007744|PDB:2OK8

Chain	Residue	Details
A	LYS13
B	LYS13
C	LYS13
D	LYS13
E	LYS13
F	LYS13

---

site_id	SWS_FT_FI2
Number of Residues	24
Details	BINDING: BINDING => ECO:0000269|PubMed:17258767, ECO:0000269|PubMed:19736991, ECO:0007744|PDB:2OK7, ECO:0007744|PDB:2OK8, ECO:0007744|PDB:3JQP, ECO:0007744|PDB:3JQQ, ECO:0007744|PDB:3JQR

Chain	Residue	Details
A	ALA100
C	ALA117
C	TYR137
C	TYR316
D	ALA100
D	ALA117
D	TYR137
D	TYR316
E	ALA100
E	ALA117
E	TYR137
A	ALA117
E	TYR316
F	ALA100
F	ALA117
F	TYR137
F	TYR316
A	TYR137
A	TYR316
B	ALA100
B	ALA117
B	TYR137
B	TYR316
C	ALA100

---

site_id	SWS_FT_FI3
Number of Residues	24
Details	BINDING: BINDING => ECO:0000305|PubMed:17258767, ECO:0000305|PubMed:19736991, ECO:0007744|PDB:2OK7, ECO:0007744|PDB:3JQP, ECO:0007744|PDB:3JQQ

Chain	Residue	Details
A	LYS119
C	SER247
C	TYR258
C	LYS286
D	LYS119
D	SER247
D	TYR258
D	LYS286
E	LYS119
E	SER247
E	TYR258
A	SER247
E	LYS286
F	LYS119
F	SER247
F	TYR258
F	LYS286
A	TYR258
A	LYS286
B	LYS119
B	SER247
B	TYR258
B	LYS286
C	LYS119

---

site_id	SWS_FT_FI4
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269|PubMed:19736991, ECO:0007744|PDB:3JQP

Chain	Residue	Details
A	THR180
B	THR180
C	THR180
D	THR180
E	THR180
F	THR180

---

site_id	SWS_FT_FI5
Number of Residues	6
Details	BINDING: BINDING => ECO:0000305|PubMed:17258767, ECO:0000305|PubMed:19736991, ECO:0007744|PDB:2OK7, ECO:0007744|PDB:3JQP

Chain	Residue	Details
A	VAL217
B	VAL217
C	VAL217
D	VAL217
E	VAL217
F	VAL217

---

site_id	SWS_FT_FI6
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269|PubMed:19736991, ECO:0007744|PDB:3JQQ

Chain	Residue	Details
A	LYS287
B	LYS287
C	LYS287
D	LYS287
E	LYS287
F	LYS287

---