5UQF

Crystal Structure of the Catalytic Domain of the Inosine Monophosphate Dehydrogenase from Campylobacter jejuni in the complex with IMP and the inhibitor P225

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0003938	molecular_function	IMP dehydrogenase activity
A	0006164	biological_process	purine nucleotide biosynthetic process
A	0016491	molecular_function	oxidoreductase activity
B	0003824	molecular_function	catalytic activity
B	0003938	molecular_function	IMP dehydrogenase activity
B	0006164	biological_process	purine nucleotide biosynthetic process
B	0016491	molecular_function	oxidoreductase activity
C	0003824	molecular_function	catalytic activity
C	0003938	molecular_function	IMP dehydrogenase activity
C	0006164	biological_process	purine nucleotide biosynthetic process
C	0016491	molecular_function	oxidoreductase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	18
Details	binding site for residue IMP A 500

Chain	Residue
A	ALA46
A	GLY357
A	SER358
A	TYR381
A	GLY383
A	MET384
A	GLY385
A	GLU411
A	8KY501
A	EDO506
A	MET48
A	GLY298
A	SER299
A	ILE300
A	CYS301
A	ASP334
A	GLY335
A	GLY336

---

site_id	AC2
Number of Residues	9
Details	binding site for residue 8KY A 501

Chain	Residue
A	SER245
A	ALA246
A	THR303
A	VAL409
A	GLU411
A	SER436
A	TYR440
A	IMP500
A	EDO506

---

site_id	AC3
Number of Residues	7
Details	binding site for residue K A 502

Chain	Residue
A	GLY296
A	GLY298
A	CYS301
A	GLU465
A	SER466
A	HIS467
A	HOH609

---

site_id	AC4
Number of Residues	5
Details	binding site for residue SO4 A 503

Chain	Residue
A	TYR373
A	TYR373
A	GLN374
A	GLN374
A	ARG416

---

site_id	AC5
Number of Residues	2
Details	binding site for residue SO4 A 504

Chain	Residue
A	HIS54
A	ARG55

---

site_id	AC6
Number of Residues	2
Details	binding site for residue SO4 A 505

Chain	Residue
A	GLN226
A	ARG229

---

site_id	AC7
Number of Residues	9
Details	binding site for residue EDO A 506

Chain	Residue
A	ALA246
A	GLY294
A	ILE295
A	GLY296
A	CYS301
A	THR303
A	TYR440
A	IMP500
A	8KY501

---

site_id	AC8
Number of Residues	1
Details	binding site for residue EDO A 507

Chain	Residue
A	ARG84

---

site_id	AC9
Number of Residues	1
Details	binding site for residue EDO A 508

Chain	Residue
A	ARG62

---

site_id	AD1
Number of Residues	3
Details	binding site for residue EDO A 509

Chain	Residue
A	TYR378
A	ARG416
A	THR472

---

site_id	AD2
Number of Residues	19
Details	binding site for residue IMP B 500

Chain	Residue
B	ALA46
B	MET48
B	GLY298
B	SER299
B	ILE300
B	CYS301
B	ASP334
B	GLY335
B	GLY336
B	MET355
B	GLY357
B	SER358
B	TYR381
B	GLY383
B	MET384
B	GLY385
B	GLU411
B	8KY501
B	HOH603

---

site_id	AD3
Number of Residues	10
Details	binding site for residue 8KY B 501

Chain	Residue
B	PRO24
B	SER245
B	THR303
B	MET384
B	GLY385
B	VAL409
B	GLU411
B	SER436
B	GLY439
B	IMP500

---

site_id	AD4
Number of Residues	6
Details	binding site for residue K B 502

Chain	Residue
B	GLY296
B	GLY298
B	CYS301
B	GLU465
B	SER466
B	HIS467

---

site_id	AD5
Number of Residues	4
Details	binding site for residue SO4 B 503

Chain	Residue
B	ILE75
B	GLN226
B	ARG229
B	HOH613

---

site_id	AD6
Number of Residues	4
Details	binding site for residue SO4 B 504

Chain	Residue
C	GLN374
B	TYR373
B	GLN374
C	TYR373

---

site_id	AD7
Number of Residues	4
Details	binding site for residue SO4 B 505

Chain	Residue
B	ARG376
B	TYR378
B	ARG416
B	THR472

---

site_id	AD8
Number of Residues	2
Details	binding site for residue SO4 B 506

Chain	Residue
B	HIS54
B	ARG55

---

site_id	AD9
Number of Residues	4
Details	binding site for residue SO4 B 507

Chain	Residue
B	LYS32
B	ASN325
B	VAL329
B	PRO330

---

site_id	AE1
Number of Residues	2
Details	binding site for residue GOL B 508

Chain	Residue
B	SER422
B	ARG424

---

site_id	AE2
Number of Residues	6
Details	binding site for residue EDO B 509

Chain	Residue
B	ARG16
B	PRO17
B	VAL441
B	ARG452
B	ALA453
B	GLU454

---

site_id	AE3
Number of Residues	6
Details	binding site for residue EDO B 510

Chain	Residue
B	PHE10
B	GLU11
B	ILE305
B	GLY341
B	ASP342
B	LYS345

---

site_id	AE4
Number of Residues	17
Details	binding site for residue IMP C 501

Chain	Residue
C	ALA46
C	MET48
C	GLY298
C	SER299
C	ILE300
C	CYS301
C	ASP334
C	GLY335
C	GLY336
C	GLY357
C	SER358
C	TYR381
C	GLY383
C	MET384
C	GLY385
C	GLU411
C	8KY502

---

site_id	AE5
Number of Residues	10
Details	binding site for residue 8KY C 502

Chain	Residue
C	LEU23
C	HIS247
C	THR303
C	MET384
C	GLY385
C	GLU411
C	SER436
C	GLY439
C	TYR440
C	IMP501

---

site_id	AE6
Number of Residues	6
Details	binding site for residue K C 503

Chain	Residue
C	GLY296
C	GLY298
C	CYS301
C	GLU465
C	SER466
C	HIS467

---

site_id	AE7
Number of Residues	3
Details	binding site for residue SO4 C 504

Chain	Residue
C	GLN226
C	ARG229
C	HOH612

---

site_id	AE8
Number of Residues	3
Details	binding site for residue SO4 C 505

Chain	Residue
C	TYR378
C	ARG416
C	THR472

---

site_id	AE9
Number of Residues	6
Details	binding site for residue GOL C 506

Chain	Residue
B	ARG416
B	THR474
C	PHE371
C	TYR373
C	ARG416
C	THR474

---

site_id	AF1
Number of Residues	2
Details	binding site for residue CL C 507

Chain	Residue
C	HIS54
C	ARG55

---

site_id	AF2
Number of Residues	1
Details	binding site for residue CL C 508

Chain	Residue
C	ARG62

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	VAL291-THR303

---