1JR1

Crystal structure of Inosine Monophosphate Dehydrogenase in complex with Mycophenolic Acid

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0003824	molecular_function	catalytic activity
A	0003938	molecular_function	IMP dehydrogenase activity
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006164	biological_process	purine nucleotide biosynthetic process
A	0006177	biological_process	GMP biosynthetic process
A	0006183	biological_process	GTP biosynthetic process
A	0007623	biological_process	circadian rhythm
A	0016491	molecular_function	oxidoreductase activity
A	0046651	biological_process	lymphocyte proliferation
A	0046872	molecular_function	metal ion binding
A	0071353	biological_process	cellular response to interleukin-4
A	0097294	biological_process	'de novo' XMP biosynthetic process
B	0000166	molecular_function	nucleotide binding
B	0003824	molecular_function	catalytic activity
B	0003938	molecular_function	IMP dehydrogenase activity
B	0005634	cellular_component	nucleus
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006164	biological_process	purine nucleotide biosynthetic process
B	0006177	biological_process	GMP biosynthetic process
B	0006183	biological_process	GTP biosynthetic process
B	0007623	biological_process	circadian rhythm
B	0016491	molecular_function	oxidoreductase activity
B	0046651	biological_process	lymphocyte proliferation
B	0046872	molecular_function	metal ion binding
B	0071353	biological_process	cellular response to interleukin-4
B	0097294	biological_process	'de novo' XMP biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE K A 601

Chain	Residue
A	GLY326
A	CYS327
A	GLY328
A	CYS331
A	GLU500
A	GLY501
A	GLY502

---

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE K B 602

Chain	Residue
B	CYS331
B	GLU500
B	GLY501
B	GLY502
B	GLY326
B	GLY328

---

site_id	AC3
Number of Residues	22
Details	BINDING SITE FOR RESIDUE IMP A 1331

Chain	Residue
A	SER68
A	MET70
A	ARG322
A	GLY328
A	SER329
A	CYS331
A	ASP364
A	GLY366
A	MET386
A	GLY387
A	SER388
A	TYR411
A	GLY413
A	MET414
A	GLY415
A	GLN441
A	GLY442
A	HOH617
A	HOH653
A	HOH664
A	HOH738
A	MOA1332

---

site_id	AC4
Number of Residues	22
Details	BINDING SITE FOR RESIDUE IMP B 1332

Chain	Residue
B	SER68
B	MET70
B	ARG322
B	GLY328
B	SER329
B	CYS331
B	ASP364
B	GLY366
B	MET385
B	GLY387
B	SER388
B	TYR411
B	GLY413
B	MET414
B	GLY415
B	GLN441
B	GLY442
B	HOH708
B	HOH710
B	HOH714
B	HOH794
B	MOA1333

---

site_id	AC5
Number of Residues	15
Details	BINDING SITE FOR RESIDUE MOA A 1332

Chain	Residue
A	ASP274
A	SER275
A	SER276
A	ASN303
A	GLY324
A	MET325
A	GLY326
A	CYS331
A	THR333
A	MET414
A	GLY415
A	GLN441
A	HOH658
A	HOH773
A	IMP1331

---

site_id	AC6
Number of Residues	13
Details	BINDING SITE FOR RESIDUE MOA B 1333

Chain	Residue
B	ASP274
B	SER275
B	SER276
B	ASN303
B	GLY324
B	MET325
B	GLY326
B	THR333
B	GLY415
B	GLN441
B	HOH725
B	HOH770
B	IMP1332

---

Functional Information from PROSITE/UniProt

site_id	PS00487
Number of Residues	13
Details	IMP_DH_GMP_RED IMP dehydrogenase / GMP reductase signature. LRVGMGcGSICiT

Chain	Residue	Details
A	LEU321-THR333

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Thioimidate intermediate

Chain	Residue	Details
A	CYS331
B	CYS331

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_03156

Chain	Residue	Details
A	ARG429
B	ARG429

---

site_id	SWS_FT_FI3
Number of Residues	10
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03156

Chain	Residue	Details
A	ASP274
B	GLY502
A	GLY324
A	GLU500
A	GLY501
A	GLY502
B	ASP274
B	GLY324
B	GLU500
B	GLY501

---

site_id	SWS_FT_FI4
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269|PubMed:8681386, ECO:0007744|PDB:1JR1

Chain	Residue	Details
A	SER276
A	GLY326
A	THR333
B	SER276
B	GLY326
B	THR333

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	BINDING: in other chain => ECO:0000255|HAMAP-Rule:MF_03156

Chain	Residue	Details
A	GLY328
A	CYS331
B	GLY328
B	CYS331

---

site_id	SWS_FT_FI6
Number of Residues	10
Details	BINDING:

Chain	Residue	Details
A	SER329
B	GLN441
A	ASP364
A	GLY387
A	TYR411
A	GLN441
B	SER329
B	ASP364
B	GLY387
B	TYR411

---

site_id	SWS_FT_FI7
Number of Residues	6
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P12268

Chain	Residue	Details
A	SER122
A	SER160
A	SER416
B	SER122
B	SER160
B	SER416

---

site_id	SWS_FT_FI8
Number of Residues	2
Details	MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P12268

Chain	Residue	Details
A	TYR400
B	TYR400

---

site_id	SWS_FT_FI9
Number of Residues	2
Details	MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P12268

Chain	Residue	Details
A	LYS511
B	LYS511

---

site_id	SWS_FT_FI10
Number of Residues	8
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0000250|UniProtKB:P12268

Chain	Residue	Details
A	LYS195
A	LYS208
A	LYS438
B	LYS195
B	LYS208
B	LYS438

---