3JQP

Crystal structure of the H286L mutant of Ferredoxin-NADP+ reductase from Plasmodium falciparum 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	18
Details	BINDING SITE FOR RESIDUE FAD A 415

Chain	Residue
A	ARG101
A	GLY136
A	TYR137
A	CYS138
A	SER139
A	THR180
A	GLU314
A	TYR316
B	LEU102
B	FAD415
A	LEU102
A	TYR103
A	SER104
A	ALA117
A	LYS119
A	HIS121
A	LYS122
A	TYR123

---

site_id	AC2
Number of Residues	15
Details	BINDING SITE FOR RESIDUE A2P A 416

Chain	Residue
A	LYS119
A	THR178
A	GLY179
A	GLY216
A	VAL217
A	TYR218
A	SER247
A	TYR258
A	GLN260
A	LEU286
A	SER288
B	TYR258
B	LYS287
B	SER288
B	A2P416

---

site_id	AC3
Number of Residues	19
Details	BINDING SITE FOR RESIDUE FAD B 415

Chain	Residue
A	LEU102
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	GLU314
B	TYR316
B	HOH320

---

site_id	AC4
Number of Residues	14
Details	BINDING SITE FOR RESIDUE A2P B 416

Chain	Residue
A	TYR258
A	SER288
A	A2P416
B	ASN33
B	LYS119
B	GLY179
B	GLY216
B	VAL217
B	TYR218
B	SER247
B	TYR258
B	GLN260
B	SER288
B	HOH317

---

site_id	AC5
Number of Residues	19
Details	BINDING SITE FOR RESIDUE FAD C 415

Chain	Residue
C	ARG101
C	LEU102
C	TYR103
C	SER104
C	ALA117
C	ILE118
C	LYS119
C	HIS121
C	LYS122
C	TYR123
C	GLY136
C	TYR137
C	CYS138
C	SER139
C	THR180
C	GLU314
C	TYR316
D	LEU102
D	FAD415

---

site_id	AC6
Number of Residues	14
Details	BINDING SITE FOR RESIDUE A2P C 416

Chain	Residue
C	LYS119
C	GLY179
C	GLY216
C	VAL217
C	TYR218
C	SER247
C	TYR258
C	GLN260
C	LEU286
C	SER288
D	TYR258
D	LYS287
D	SER288
D	A2P416

---

site_id	AC7
Number of Residues	18
Details	BINDING SITE FOR RESIDUE FAD D 415

Chain	Residue
C	LEU102
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	GLU314
D	TYR316

---

site_id	AC8
Number of Residues	17
Details	BINDING SITE FOR RESIDUE A2P D 416

Chain	Residue
C	TYR258
C	LYS287
C	SER288
C	A2P416
D	ASN33
D	LYS119
D	THR178
D	GLY179
D	GLY216
D	VAL217
D	TYR218
D	SER247
D	TYR258
D	GLN260
D	LEU286
D	SER288
D	HOH317

---

site_id	AC9
Number of Residues	16
Details	BINDING SITE FOR RESIDUE FAD E 415

Chain	Residue
E	ARG101
E	LEU102
E	TYR103
E	SER104
E	ALA117
E	LYS119
E	HIS121
E	TYR123
E	GLY136
E	TYR137
E	CYS138
E	SER139
E	THR180
E	TYR316
F	LEU102
F	FAD415

---

site_id	BC1
Number of Residues	14
Details	BINDING SITE FOR RESIDUE A2P E 416

Chain	Residue
E	LYS119
E	THR178
E	GLY216
E	VAL217
E	TYR218
E	SER247
E	TYR258
E	GLN260
E	LEU286
E	SER288
F	TYR258
F	LYS287
F	SER288
F	A2P416

---

site_id	BC2
Number of Residues	18
Details	BINDING SITE FOR RESIDUE FAD F 415

Chain	Residue
E	LEU102
E	FAD415
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	SER183
F	TYR316

---

site_id	BC3
Number of Residues	15
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	LEU286
F	SER288
F	HOH332
F	HOH337

---

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	LEU286
D	LYS119
D	SER247
D	TYR258
D	LEU286
E	LYS119
E	SER247
E	TYR258
A	SER247
E	LEU286
F	LYS119
F	SER247
F	TYR258
F	LEU286
A	TYR258
A	LEU286
B	LYS119
B	SER247
B	TYR258
B	LEU286
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

---