6VFZ

Crystal Structure of Human Mitochondrial Isocitrate Dehydrogenase (IDH2) R140Q Mutant Homodimer in Complex with NADPH and AG-881 (Vorasidenib) Inhibitor.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0004450	molecular_function	isocitrate dehydrogenase (NADP+) activity
A	0005739	cellular_component	mitochondrion
A	0005759	cellular_component	mitochondrial matrix
A	0005777	cellular_component	peroxisome
A	0005829	cellular_component	cytosol
A	0005975	biological_process	carbohydrate metabolic process
A	0006097	biological_process	glyoxylate cycle
A	0006099	biological_process	tricarboxylic acid cycle
A	0006102	biological_process	isocitrate metabolic process
A	0006103	biological_process	2-oxoglutarate metabolic process
A	0006739	biological_process	NADP+ metabolic process
A	0006741	biological_process	NADP+ biosynthetic process
A	0016491	molecular_function	oxidoreductase activity
A	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A	0046872	molecular_function	metal ion binding
A	0051287	molecular_function	NAD binding
A	0060253	biological_process	negative regulation of glial cell proliferation
A	0070062	cellular_component	extracellular exosome
A	1903976	biological_process	negative regulation of glial cell migration
A	1904465	biological_process	negative regulation of matrix metallopeptidase secretion
B	0000287	molecular_function	magnesium ion binding
B	0004450	molecular_function	isocitrate dehydrogenase (NADP+) activity
B	0005739	cellular_component	mitochondrion
B	0005759	cellular_component	mitochondrial matrix
B	0005777	cellular_component	peroxisome
B	0005829	cellular_component	cytosol
B	0005975	biological_process	carbohydrate metabolic process
B	0006097	biological_process	glyoxylate cycle
B	0006099	biological_process	tricarboxylic acid cycle
B	0006102	biological_process	isocitrate metabolic process
B	0006103	biological_process	2-oxoglutarate metabolic process
B	0006739	biological_process	NADP+ metabolic process
B	0006741	biological_process	NADP+ biosynthetic process
B	0016491	molecular_function	oxidoreductase activity
B	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B	0046872	molecular_function	metal ion binding
B	0051287	molecular_function	NAD binding
B	0060253	biological_process	negative regulation of glial cell proliferation
B	0070062	cellular_component	extracellular exosome
B	1903976	biological_process	negative regulation of glial cell migration
B	1904465	biological_process	negative regulation of matrix metallopeptidase secretion

Functional Information from PDB Data

site_id	AC1
Number of Residues	18
Details	binding site for residue 9UO A 501

Chain	Residue
A	TRP164
B	TRP164
B	VAL294
B	VAL297
B	LEU298
B	ASP312
B	VAL315
B	GLN316
B	ILE319
B	LEU320
A	VAL294
A	VAL297
A	LEU298
A	ASP312
A	VAL315
A	GLN316
A	ILE319
A	LEU320

---

site_id	AC2
Number of Residues	24
Details	binding site for residue NDP A 502

Chain	Residue
A	LYS112
A	ALA114
A	THR115
A	ILE116
A	THR117
A	ARG122
A	ASN136
A	GLU345
A	HIS348
A	GLY349
A	THR350
A	VAL351
A	THR352
A	ARG353
A	HIS354
A	THR366
A	ASN367
A	HOH676
A	HOH709
A	HOH743
A	HOH748
A	HOH750
A	HOH756
A	HOH776

---

site_id	AC3
Number of Residues	6
Details	binding site for residue CA A 503

Chain	Residue
A	ASP314
A	ASP318
A	HOH710
A	HOH739
A	HOH884
B	ASP291

---

site_id	AC4
Number of Residues	4
Details	binding site for residue NA A 504

Chain	Residue
A	ARG149
A	ILE170
A	SER317
A	HOH924

---

site_id	AC5
Number of Residues	21
Details	binding site for residue NDP B 501

Chain	Residue
B	LYS112
B	THR115
B	ILE116
B	THR117
B	ARG122
B	ASN136
B	GLU345
B	HIS348
B	GLY349
B	THR350
B	VAL351
B	THR352
B	ARG353
B	HIS354
B	THR366
B	ASN367
B	HOH650
B	HOH668
B	HOH725
B	HOH733
B	HOH777

---

site_id	AC6
Number of Residues	6
Details	binding site for residue CA B 502

Chain	Residue
A	ASP291
B	ASP314
B	ASP318
B	HOH696
B	HOH772
B	HOH778

---

site_id	AC7
Number of Residues	4
Details	binding site for residue NA B 503

Chain	Residue
B	ARG149
B	ILE170
B	SER317
B	HOH830

---

Functional Information from PROSITE/UniProt

site_id	PS00470
Number of Residues	20
Details	IDH_IMDH Isocitrate and isopropylmalate dehydrogenases signature. NYDGDVqSDilAqgf.GSLGL

Chain	Residue	Details
A	ASN310-LEU329

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	20
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"O75874","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	22
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P33198","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	Site: {"description":"Critical for catalysis","evidences":[{"source":"UniProtKB","id":"P33198","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	12
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P54071","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	12
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	16
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P54071","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"22416140","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---