Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4ZQR

Crystal Structure of the Catalytic Domain of the Inosine Monophosphate Dehydrogenase from Mycobacterium tuberculosis

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
D	0003824	molecular_function	catalytic activity
D	0003938	molecular_function	IMP dehydrogenase activity
D	0006164	biological_process	purine nucleotide biosynthetic process
D	0016491	molecular_function	oxidoreductase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	10
Details	binding site for residue PO4 A 601

Chain	Residue
A	GLY338
A	HOH758
A	SER339
A	GLY376
A	GLY397
A	SER398
A	TYR421
A	HOH720
A	HOH722
A	HOH741

site_id	AC2
Number of Residues	6
Details	binding site for residue PGO A 602

Chain	Residue
A	PRO61
A	ALA483
A	GLY486
A	TYR487
D	GLU458
D	PGO604

site_id	AC3
Number of Residues	7
Details	binding site for residue PGO A 603

Chain	Residue
A	ALA285
A	HIS286
A	ASN289
A	ASP453
A	HOH753
A	HOH827
C	PGO603

site_id	AC4
Number of Residues	4
Details	binding site for residue PGO A 604

Chain	Residue
A	ARG482
A	PGO605
C	MET271
C	ASP274

site_id	AC5
Number of Residues	6
Details	binding site for residue PGO A 605

Chain	Residue
A	THR63
A	ALA64
A	ARG482
A	PGO604
A	HOH764
C	TRP266

site_id	AC6
Number of Residues	5
Details	binding site for residue GOL A 606

Chain	Residue
A	GLN378
A	LEU399
A	GLN476
A	TYR527
A	HOH808

site_id	AC7
Number of Residues	9
Details	binding site for residue GOL A 607

Chain	Residue
A	ASP48
A	ASP49
A	ILE504
A	THR505
A	PRO506
A	LEU509
C	THR505
C	PRO506
C	ALA507

site_id	AC8
Number of Residues	8
Details	binding site for residue GOL A 608

Chain	Residue
A	ASP48
A	GLN378
A	TYR379
A	ASP382
A	HOH771
C	LYS510
C	HIS515
C	ASP516

site_id	AC9
Number of Residues	6
Details	binding site for residue K A 609

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

site_id	AD1
Number of Residues	6
Details	binding site for residue GOL A 610

Chain	Residue
A	PRO506
A	HOH703
B	PRO506
C	PRO506
D	PRO506
D	PGO601

site_id	AD2
Number of Residues	6
Details	binding site for residue K A 611

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

site_id	AD3
Number of Residues	11
Details	binding site for residue PO4 B 601

Chain	Residue
B	GLY338
B	SER339
B	GLY375
B	GLY376
B	GLY397
B	SER398
B	TYR421
B	HOH728
B	HOH733
B	HOH738
B	HOH771

site_id	AD4
Number of Residues	7
Details	binding site for residue PGO B 602

Chain	Residue
B	PRO61
B	ALA483
B	GLY486
B	TYR487
C	GLU458
C	GOL604
C	HOH739

site_id	AD5
Number of Residues	4
Details	binding site for residue PGO B 603

Chain	Residue
B	ALA285
B	HIS286
B	ASN289
B	HOH735

site_id	AD6
Number of Residues	6
Details	binding site for residue GOL B 604

Chain	Residue
B	HOH709
B	HOH838
B	GLN378
B	TYR379
B	LEU399
B	TYR527

site_id	AD7
Number of Residues	6
Details	binding site for residue K B 605

Chain	Residue
B	GLU511
B	SER512
B	HIS513
C	GLY336
C	GLY338
C	CYS341

site_id	AD8
Number of Residues	5
Details	binding site for residue PGO B 606

Chain	Residue
B	GLU458
D	PRO61
D	ALA483
D	GLY486
D	TYR487

site_id	AD9
Number of Residues	7
Details	binding site for residue PGO B 607

Chain	Residue
B	ASP49
B	THR505
B	PRO506
B	HOH874
D	THR505
D	PRO506
D	ALA507

site_id	AE1
Number of Residues	8
Details	binding site for residue GOL B 608

Chain	Residue
B	ASP48
B	GLN378
B	TYR379
B	ASP382
B	HOH820
D	LYS510
D	HIS515
D	ASP516

site_id	AE2
Number of Residues	6
Details	binding site for residue K B 609

Chain	Residue
B	GLY336
B	GLY338
B	CYS341
D	GLU511
D	SER512
D	HIS513

site_id	AE3
Number of Residues	7
Details	binding site for residue PGO C 601

Chain	Residue
B	THR505
B	PRO506
B	ALA507
C	ASP48
C	ASP49
C	PRO506
C	HOH822

site_id	AE4
Number of Residues	10
Details	binding site for residue PO4 C 602

Chain	Residue
C	GLY338
C	SER339
C	GLY376
C	GLY397
C	SER398
C	TYR421
C	HOH735
C	HOH737
C	HOH738
C	HOH764

site_id	AE5
Number of Residues	6
Details	binding site for residue PGO C 603

Chain	Residue
A	GLU458
A	PGO603
A	HOH717
C	ALA483
C	GLY486
C	TYR487

site_id	AE6
Number of Residues	6
Details	binding site for residue GOL C 604

Chain	Residue
B	PGO602
C	ALA285
C	HIS286
C	ASN289
C	HOH741
C	HOH814

site_id	AE7
Number of Residues	4
Details	binding site for residue GOL C 605

Chain	Residue
C	ASP65
C	SER67
C	ARG75
C	HOH729

site_id	AE8
Number of Residues	8
Details	binding site for residue GOL C 606

Chain	Residue
B	LYS510
B	HIS515
B	ASP516
C	ASP48
C	GLN378
C	TYR379
C	ASP382
C	HOH794

site_id	AE9
Number of Residues	6
Details	binding site for residue PGO C 607

Chain	Residue
C	GLN378
C	TYR379
C	LEU399
C	TYR527
C	HOH702
C	HOH833

site_id	AF1
Number of Residues	10
Details	binding site for residue PGO D 601

Chain	Residue
A	THR505
A	PRO506
A	ALA507
A	GOL610
D	ASP48
D	ASP49
D	THR505
D	PRO506
D	LEU509
D	HOH710

site_id	AF2
Number of Residues	8
Details	binding site for residue GOL D 602

Chain	Residue
A	LYS510
A	HIS515
A	ASP516
D	ASP48
D	GLN378
D	TYR379
D	ASP382
D	HOH826

site_id	AF3
Number of Residues	11
Details	binding site for residue PO4 D 603

Chain	Residue
D	GLY338
D	SER339
D	GLY375
D	GLY376
D	GLY397
D	SER398
D	TYR421
D	HOH718
D	HOH723
D	HOH734
D	HOH774

site_id	AF4
Number of Residues	7
Details	binding site for residue PGO D 604

Chain	Residue
A	PGO602
A	HOH802
D	ALA285
D	HIS286
D	ASN289
D	ASP453
D	HOH827

site_id	AF5
Number of Residues	3
Details	binding site for residue PGO D 605

Chain	Residue
A	MET271
A	ASP274
D	PGO606

site_id	AF6
Number of Residues	6
Details	binding site for residue PGO D 606

Chain	Residue
A	TRP266
D	THR63
D	ALA64
D	ARG482
D	PGO605
D	HOH837

site_id	AF7
Number of Residues	6
Details	binding site for residue GOL D 607

Chain	Residue
D	GLN378
D	TYR379
D	LEU399
D	TYR527
D	HOH703
D	HOH745

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	4
Details	ACT_SITE: Thioimidate intermediate => ECO:0000255\|HAMAP-Rule:MF_01964, ECO:0000305\|PubMed:26440283

Chain	Residue	Details
A	CYS341
B	CYS341
C	CYS341
D	CYS341

site_id	SWS_FT_FI2
Number of Residues	4
Details	ACT_SITE: Proton acceptor => ECO:0000255\|HAMAP-Rule:MF_01964, ECO:0000305\|PubMed:26440283

Chain	Residue	Details
A	ARG443
B	ARG443
C	ARG443
D	ARG443

site_id	SWS_FT_FI3
Number of Residues	32
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_01964, ECO:0000269\|PubMed:26440283

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

site_id	SWS_FT_FI4
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269\|PubMed:26440283

Chain	Residue	Details
A	ASN289
D	ASN289
D	THR343
D	GLU458
A	THR343
A	GLU458
B	ASN289
B	THR343
B	GLU458
C	ASN289
C	THR343
C	GLU458

site_id	SWS_FT_FI5
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_01964

Chain	Residue	Details
A	GLY334
B	GLY334
C	GLY334
D	GLY334

site_id	SWS_FT_FI6
Number of Residues	12
Details	BINDING: in other chain => ECO:0000255\|HAMAP-Rule:MF_01964, ECO:0000269\|PubMed:26440283

Chain	Residue	Details
A	GLY336
D	GLY336
D	GLY338
D	CYS341
A	GLY338
A	CYS341
B	GLY336
B	GLY338
B	CYS341
C	GLY336
C	GLY338
C	CYS341

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)