1J1W

Crystal Structure Of The Monomeric Isocitrate Dehydrogenase In Complex With NADP+

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004450	molecular_function	isocitrate dehydrogenase (NADP+) activity
A	0005737	cellular_component	cytoplasm
A	0006097	biological_process	glyoxylate cycle
A	0006099	biological_process	tricarboxylic acid cycle
A	0016491	molecular_function	oxidoreductase activity
A	0046872	molecular_function	metal ion binding
B	0004450	molecular_function	isocitrate dehydrogenase (NADP+) activity
B	0005737	cellular_component	cytoplasm
B	0006097	biological_process	glyoxylate cycle
B	0006099	biological_process	tricarboxylic acid cycle
B	0016491	molecular_function	oxidoreductase activity
B	0046872	molecular_function	metal ion binding
C	0004450	molecular_function	isocitrate dehydrogenase (NADP+) activity
C	0005737	cellular_component	cytoplasm
C	0006097	biological_process	glyoxylate cycle
C	0006099	biological_process	tricarboxylic acid cycle
C	0016491	molecular_function	oxidoreductase activity
C	0046872	molecular_function	metal ion binding
D	0004450	molecular_function	isocitrate dehydrogenase (NADP+) activity
D	0005737	cellular_component	cytoplasm
D	0006097	biological_process	glyoxylate cycle
D	0006099	biological_process	tricarboxylic acid cycle
D	0016491	molecular_function	oxidoreductase activity
D	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	19
Details	BINDING SITE FOR RESIDUE NAP A 1000

Chain	Residue
A	LYS82
A	GLY584
A	SER585
A	ALA586
A	PRO587
A	HIS589
A	ARG600
A	TRP601
A	ASP602
A	ARG649
A	HOH3021
A	PRO84
A	ASN85
A	SER87
A	ASN135
A	ASP346
A	ALA351
A	ALA563
A	GLY583

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site_id	AC2
Number of Residues	19
Details	BINDING SITE FOR RESIDUE NAP B 1001

Chain	Residue
B	LYS82
B	PRO84
B	ASN85
B	SER87
B	ASN135
B	ARG139
B	ILE348
B	ALA351
B	ALA563
B	GLY583
B	GLY584
B	SER585
B	ALA586
B	HIS589
B	ARG600
B	TRP601
B	ASP602
B	ARG649
B	HOH3104

---

site_id	AC3
Number of Residues	17
Details	BINDING SITE FOR RESIDUE NAP C 1002

Chain	Residue
C	LYS82
C	PRO84
C	ASN85
C	SER87
C	ASN135
C	ASP346
C	ALA351
C	ALA563
C	GLY583
C	GLY584
C	SER585
C	ALA586
C	HIS589
C	ARG600
C	TRP601
C	ASP602
C	ARG649

---

site_id	AC4
Number of Residues	19
Details	BINDING SITE FOR RESIDUE NAP D 1003

Chain	Residue
D	LYS82
D	PRO84
D	ASN85
D	SER87
D	ASN135
D	ALA351
D	ALA563
D	GLY583
D	GLY584
D	SER585
D	ALA586
D	HIS589
D	ARG600
D	TRP601
D	ASP602
D	ARG649
D	HOH3010
D	HOH3041
D	HOH3321

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	32
Details	BINDING: BINDING => ECO:0000269|PubMed:12855708, ECO:0007744|PDB:1J1W

Chain	Residue	Details
A	ASN85
B	SER87
B	ASN135
B	SER585
B	HIS589
B	ARG600
B	ASP602
B	ARG649
C	ASN85
C	SER87
C	ASN135
A	SER87
C	SER585
C	HIS589
C	ARG600
C	ASP602
C	ARG649
D	ASN85
D	SER87
D	ASN135
D	SER585
D	HIS589
A	ASN135
D	ARG600
D	ASP602
D	ARG649
A	SER585
A	HIS589
A	ARG600
A	ASP602
A	ARG649
B	ASN85

---

site_id	SWS_FT_FI2
Number of Residues	32
Details	BINDING: BINDING => ECO:0000269|PubMed:12467571, ECO:0007744|PDB:1ITW

Chain	Residue	Details
A	SER132
B	ARG139
B	ARG145
B	LYS255
B	ASP350
B	TYR420
B	ARG547
B	ASP548
C	SER132
C	ARG139
C	ARG145
A	ARG139
C	LYS255
C	ASP350
C	TYR420
C	ARG547
C	ASP548
D	SER132
D	ARG139
D	ARG145
D	LYS255
D	ASP350
A	ARG145
D	TYR420
D	ARG547
D	ASP548
A	LYS255
A	ASP350
A	TYR420
A	ARG547
A	ASP548
B	SER132

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