4ZQO

Crystal Structure of the Catalytic Domain of the Inosine Monophosphate Dehydrogenase from Mycobacterium tuberculosis in the complex with IMP and the inhibitor Q67

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	25
Details	binding site for residue IMP A 601

Chain	Residue
A	SER83
A	GLY376
A	MET395
A	GLY397
A	SER398
A	TYR421
A	GLY423
A	MET424
A	GLY425
A	GLU458
A	GLY459
A	MET85
A	Q67602
A	HOH715
A	HOH763
A	HOH798
A	HOH821
A	HOH830
A	GLY338
A	SER339
A	ILE340
A	CYS341
A	THR343
A	ASP374
A	GLY375

---

site_id	AC2
Number of Residues	14
Details	binding site for residue Q67 A 602

Chain	Residue
A	SER57
A	VAL59
A	ALA285
A	ASN289
A	MET424
A	GLY425
A	VAL456
A	GLU458
A	ALA483
A	GLY486
A	TYR487
A	IMP601
A	HOH836
A	HOH842

---

site_id	AC3
Number of Residues	6
Details	binding site for residue K A 603

Chain	Residue
A	GLY336
A	GLY338
A	CYS341
A	GLU511
A	SER512
A	HIS513

---

site_id	AC4
Number of Residues	9
Details	binding site for residue GOL A 604

Chain	Residue
A	ASP48
A	GLN378
A	TYR379
A	ASP382
A	LYS510
A	HIS515
A	ASP516
A	HOH711
A	HOH718

---

site_id	AC5
Number of Residues	7
Details	binding site for residue PGO A 605

Chain	Residue
A	GLN69
A	GLY368
A	PRO370
A	SER392
A	HOH727
A	HOH769
A	HOH813

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	VAL331-THR343

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Thioimidate intermediate => ECO:0000255|HAMAP-Rule:MF_01964, ECO:0000305|PubMed:26440283

Chain	Residue	Details
A	CYS341

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01964, ECO:0000305|PubMed:26440283

Chain	Residue	Details
A	ARG443

---

site_id	SWS_FT_FI3
Number of Residues	8
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01964, ECO:0000269|PubMed:26440283

Chain	Residue	Details
A	ASP283
A	SER339
A	ASP374
A	GLY397
A	TYR421
A	GLU511
A	SER512
A	HIS513

---

site_id	SWS_FT_FI4
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269|PubMed:26440283

Chain	Residue	Details
A	ASN289
A	THR343
A	GLU458

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01964

Chain	Residue	Details
A	GLY334

---

site_id	SWS_FT_FI6
Number of Residues	3
Details	BINDING: in other chain => ECO:0000255|HAMAP-Rule:MF_01964, ECO:0000269|PubMed:26440283

Chain	Residue	Details
A	GLY336
A	GLY338
A	CYS341

---