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Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2OK7

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	4
Details	BINDING SITE FOR RESIDUE NA A 9001

Chain	Residue
A	THR178
A	HIS286
A	A2P416
A	HOH9028

site_id	AC2
Number of Residues	22
Details	BINDING SITE FOR RESIDUE FAD A 415

Chain	Residue
A	ILE118
A	LYS119
A	HIS121
A	LYS122
A	TYR123
A	GLY136
A	TYR137
A	CYS138
A	SER139
A	THR180
A	TYR316
A	HOH9003
A	HOH9007
A	HOH9011
A	HOH9039
B	LEU102
B	FAD415
A	ARG101
A	LEU102
A	TYR103
A	SER104
A	ALA117

site_id	AC3
Number of Residues	15
Details	BINDING SITE FOR RESIDUE A2P A 416

Chain	Residue
A	LYS119
A	GLY216
A	VAL217
A	TYR218
A	SER247
A	TYR258
A	GLN260
A	HIS286
A	SER288
A	NA9001
A	HOH9035
B	TYR258
B	LYS287
B	SER288
B	A2P416

site_id	AC4
Number of Residues	21
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	TYR316
B	HOH433
B	HOH436
B	HOH452
B	HOH463

site_id	AC5
Number of Residues	13
Details	BINDING SITE FOR RESIDUE A2P B 416

Chain	Residue
A	TYR258
A	SER288
A	A2P416
B	GLY179
B	GLY216
B	VAL217
B	TYR218
B	SER247
B	TYR258
B	GLN260
B	HIS286
B	SER288
B	HOH437

site_id	AC6
Number of Residues	24
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	TYR123
C	GLY136
C	TYR137
C	CYS138
C	SER139
C	THR180
C	GLU314
C	TYR316
C	HOH419
C	HOH423
C	HOH441
C	HOH449
C	HOH454
C	HOH457
D	LEU102
D	FAD415

site_id	AC7
Number of Residues	16
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	HIS286
C	SER288
C	HOH428
C	HOH438
C	HOH446
D	TYR258
D	LYS287
D	SER288
D	A2P416

site_id	AC8
Number of Residues	19
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	TYR316
D	HOH436
D	HOH445

site_id	AC9
Number of Residues	14
Details	BINDING SITE FOR RESIDUE A2P D 416

Chain	Residue
C	TYR258
C	LYS287
C	SER288
C	A2P416
D	GLY216
D	VAL217
D	TYR218
D	SER247
D	TYR258
D	GLN260
D	HIS286
D	SER288
D	HOH424
D	HOH433

site_id	BC1
Number of Residues	18
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	HOH424
F	LEU102
F	FAD415

site_id	BC2
Number of Residues	15
Details	BINDING SITE FOR RESIDUE A2P E 416

Chain	Residue
E	LYS119
E	THR178
E	GLY179
E	GLY216
E	VAL217
E	TYR218
E	SER247
E	TYR258
E	GLN260
E	HIS286
E	SER288
F	TYR258
F	LYS287
F	SER288
F	A2P416

site_id	BC3
Number of Residues	17
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	LYS119
F	HIS121
F	TYR123
F	GLY136
F	TYR137
F	CYS138
F	SER139
F	THR180
F	TYR316
F	HOH429

site_id	BC4
Number of Residues	16
Details	BINDING SITE FOR RESIDUE A2P F 416

Chain	Residue
E	TYR258
E	LYS287
E	SER288
E	TYR291
E	LYS292
E	A2P416
F	LYS119
F	THR178
F	GLY216
F	VAL217
F	TYR218
F	SER247
F	TYR258
F	HIS286
F	SER288
F	HOH426

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
B	TYR137
B	TYR316
C	ALA100
C	ALA117
C	TYR137
C	TYR316
D	ALA100
D	ALA117
D	TYR137
D	TYR316
E	ALA100
E	ALA117
E	TYR137
E	TYR316
F	ALA100
F	ALA117
F	TYR137
F	TYR316
A	ALA100
A	ALA117
A	TYR137
A	TYR316
B	ALA100
B	ALA117

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
D	LYS119
D	SER247
D	TYR258
D	HIS286
E	LYS119
E	SER247
E	TYR258
E	HIS286
F	LYS119
F	SER247
F	TYR258
F	HIS286
A	LYS119
A	SER247
A	TYR258
A	HIS286
B	LYS119
B	SER247
B	TYR258
B	HIS286
C	LYS119
C	SER247
C	TYR258
C	HIS286

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

221051

PDB entries from 2024-06-12

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