6LKZ

Crystal structure of isocitrate dehydrogenase 1 from Phaeodactylum tricornutum

Functional Information from GO Data

Chain	GOid	namespace	contents
C	0000287	molecular_function	magnesium ion binding
C	0004449	molecular_function	isocitrate dehydrogenase (NAD+) activity
C	0004450	molecular_function	isocitrate dehydrogenase (NADP+) activity
C	0005509	molecular_function	calcium ion binding
C	0005739	cellular_component	mitochondrion
C	0006099	biological_process	tricarboxylic acid cycle
C	0006102	biological_process	isocitrate metabolic process
C	0006739	biological_process	NADP metabolic process
C	0016491	molecular_function	oxidoreductase activity
C	0019674	biological_process	NAD metabolic process
C	0042802	molecular_function	identical protein binding
C	0042803	molecular_function	protein homodimerization activity
C	0046872	molecular_function	metal ion binding
D	0000287	molecular_function	magnesium ion binding
D	0004449	molecular_function	isocitrate dehydrogenase (NAD+) activity
D	0004450	molecular_function	isocitrate dehydrogenase (NADP+) activity
D	0005509	molecular_function	calcium ion binding
D	0005739	cellular_component	mitochondrion
D	0006099	biological_process	tricarboxylic acid cycle
D	0006102	biological_process	isocitrate metabolic process
D	0006739	biological_process	NADP metabolic process
D	0016491	molecular_function	oxidoreductase activity
D	0019674	biological_process	NAD metabolic process
D	0042802	molecular_function	identical protein binding
D	0042803	molecular_function	protein homodimerization activity
D	0046872	molecular_function	metal ion binding

Functional Information from PROSITE/UniProt

site_id	PS00018
Number of Residues	13
Details	EF_HAND_1 EF-hand calcium-binding domain. DKNGDGFIDfeEF

Chain	Residue	Details
C	ASP459-PHE471

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	22
Details	BINDING: BINDING => ECO:0000250|UniProtKB:A0A096P8D3

Chain	Residue	Details
C	THR79
C	HIS319
C	ASN338
D	THR79
D	SER98
D	ASN100
D	ARG134
D	TYR141
D	LYS213
D	ASP258
D	ASP282
C	SER98
D	ASP286
D	HIS319
D	ASN338
C	ASN100
C	ARG134
C	TYR141
C	LYS213
C	ASP258
C	ASP282
C	ASP286

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site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448

Chain	Residue	Details
C	ASP459
C	ASN461
C	ASP463
C	GLU470
D	ASP459
D	ASN461
D	ASP463
D	GLU470

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site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU10142

Chain	Residue	Details
C	PHE465
D	PHE465

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