1ITW

Crystal structure of the monomeric isocitrate dehydrogenase in complex with isocitrate and Mn

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	5
Details	BINDING SITE FOR RESIDUE MN A 742

Chain	Residue
A	ASP350
A	ASP548
A	ICT743
A	HOH850
A	HOH944

---

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN B 742

Chain	Residue
B	HOH883
B	ASP350
B	ASP548
B	ICT744
B	HOH881

---

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN B 743

Chain	Residue
B	GLU239
B	HOH1093
B	HOH1348
B	HOH1349
B	HOH1350

---

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN C 742

Chain	Residue
C	ASP350
C	ASP548
C	ICT743
C	HOH772
C	HOH1065

---

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN D 742

Chain	Residue
D	ASP350
D	ASP548
D	ICT743
D	HOH809
D	HOH896

---

site_id	AC6
Number of Residues	18
Details	BINDING SITE FOR RESIDUE ICT A 743

Chain	Residue
A	SER132
A	ASN135
A	ARG139
A	ARG145
A	LYS255
A	MET258
A	ASP350
A	TYR420
A	ARG547
A	ASP548
A	ALA582
A	MN742
A	HOH749
A	HOH752
A	HOH850
A	HOH944
A	HOH985
A	HOH1063

---

site_id	AC7
Number of Residues	17
Details	BINDING SITE FOR RESIDUE ICT B 744

Chain	Residue
B	SER132
B	ASN135
B	ARG139
B	ARG145
B	LYS255
B	MET258
B	ASP350
B	TYR420
B	ARG547
B	ASP548
B	ALA582
B	MN742
B	HOH758
B	HOH763
B	HOH883
B	HOH895
B	HOH944

---

site_id	AC8
Number of Residues	17
Details	BINDING SITE FOR RESIDUE ICT C 743

Chain	Residue
C	SER132
C	ASN135
C	ARG139
C	ARG145
C	LYS255
C	MET258
C	ASP350
C	TYR420
C	ARG547
C	ASP548
C	ALA582
C	MN742
C	HOH770
C	HOH772
C	HOH801
C	HOH1003
C	HOH1031

---

site_id	AC9
Number of Residues	17
Details	BINDING SITE FOR RESIDUE ICT D 743

Chain	Residue
D	SER132
D	ASN135
D	ARG139
D	ARG145
D	LYS255
D	MET258
D	ASP350
D	TYR420
D	ARG547
D	ASP548
D	ALA582
D	MN742
D	HOH754
D	HOH809
D	HOH820
D	HOH1123
D	HOH1203

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	36
Details	BINDING:

Chain	Residue	Details
A	LYS82
B	LYS82
B	SER132
B	ASN135
B	ARG145
B	ARG547
B	GLY584
B	HIS589
B	ARG600
B	ARG649
C	LYS82
A	SER132
C	SER132
C	ASN135
C	ARG145
C	ARG547
C	GLY584
C	HIS589
C	ARG600
C	ARG649
D	LYS82
D	SER132
A	ASN135
D	ASN135
D	ARG145
D	ARG547
D	GLY584
D	HIS589
D	ARG600
D	ARG649
A	ARG145
A	ARG547
A	GLY584
A	HIS589
A	ARG600
A	ARG649

---

site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269|PubMed:12467571, ECO:0007744|PDB:1ITW

Chain	Residue	Details
A	ASP350
A	ASP548
B	ASP350
B	ASP548
C	ASP350
C	ASP548
D	ASP350
D	ASP548

---

site_id	SWS_FT_FI3
Number of Residues	8
Details	SITE: Critical for catalysis => ECO:0000250

Chain	Residue	Details
A	LYS255
A	TYR420
B	LYS255
B	TYR420
C	LYS255
C	TYR420
D	LYS255
D	TYR420

---