Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5UUZ

Crystal Structure of the Catalytic Domain of the Inosine Monophosphate Dehydrogenase from Bacillus anthracis in the complex with IMP and the inhibitor P200

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
E	0003824	molecular_function	catalytic activity
E	0003938	molecular_function	IMP dehydrogenase activity
E	0006164	biological_process	purine nucleotide biosynthetic process
E	0016491	molecular_function	oxidoreductase activity
F	0003824	molecular_function	catalytic activity
F	0003938	molecular_function	IMP dehydrogenase activity
F	0006164	biological_process	purine nucleotide biosynthetic process
F	0016491	molecular_function	oxidoreductase activity
G	0003824	molecular_function	catalytic activity
G	0003938	molecular_function	IMP dehydrogenase activity
G	0006164	biological_process	purine nucleotide biosynthetic process
G	0016491	molecular_function	oxidoreductase activity
H	0003824	molecular_function	catalytic activity
H	0003938	molecular_function	IMP dehydrogenase activity
H	0006164	biological_process	purine nucleotide biosynthetic process
H	0016491	molecular_function	oxidoreductase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	21
Details	binding site for residue IMP A 501

Chain	Residue
A	ALA49
A	GLY343
A	MET362
A	GLY364
A	SER365
A	TYR388
A	GLY390
A	MET391
A	GLY392
A	GLU416
A	GLY417
A	MET51
A	8L4502
A	HOH612
A	ASN280
A	GLY305
A	SER306
A	ILE307
A	CYS308
A	ASP341
A	GLY342

site_id	AC2
Number of Residues	12
Details	binding site for residue 8L4 A 502

Chain	Residue
A	ALA253
A	THR310
A	MET391
A	GLY392
A	VAL414
A	GLU416
A	IMP501
A	HOH602
C	PRO27
C	ALA441
C	GLY444
C	TYR445

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

Chain	Residue
A	GLU470
A	SER471
A	HIS472
B	GLY303
B	GLY305
B	CYS308

site_id	AC4
Number of Residues	6
Details	binding site for residue K A 504

Chain	Residue
A	GLY303
A	GLY305
A	CYS308
C	GLU470
C	SER471
C	HIS472

site_id	AC5
Number of Residues	19
Details	binding site for residue IMP B 500

Chain	Residue
B	ALA49
B	MET51
B	GLY305
B	SER306
B	ILE307
B	CYS308
B	ASP341
B	GLY342
B	GLY343
B	MET362
B	GLY364
B	SER365
B	TYR388
B	GLY390
B	MET391
B	GLY392
B	GLU416
B	GLY417
B	8L4501

site_id	AC6
Number of Residues	11
Details	binding site for residue 8L4 B 501

Chain	Residue
A	PRO27
A	ALA441
A	GLY444
A	TYR445
B	ALA253
B	THR310
B	MET391
B	GLY392
B	VAL414
B	GLU416
B	IMP500

site_id	AC7
Number of Residues	6
Details	binding site for residue K B 502

Chain	Residue
B	GLU470
B	SER471
B	HIS472
D	GLY303
D	GLY305
D	CYS308

site_id	AC8
Number of Residues	21
Details	binding site for residue IMP C 501

Chain	Residue
C	8L4502
C	HOH616
C	HOH619
C	ALA49
C	MET51
C	GLY305
C	SER306
C	ILE307
C	CYS308
C	ASP341
C	GLY342
C	GLY343
C	MET362
C	GLY364
C	SER365
C	TYR388
C	GLY390
C	MET391
C	GLY392
C	GLU416
C	GLY417

site_id	AC9
Number of Residues	12
Details	binding site for residue 8L4 C 502

Chain	Residue
C	ALA253
C	THR310
C	MET391
C	GLY392
C	VAL414
C	GLU416
C	IMP501
C	HOH601
D	PRO27
D	ALA441
D	GLY444
D	TYR445

site_id	AD1
Number of Residues	6
Details	binding site for residue K C 503

Chain	Residue
C	GLY303
C	GLY305
C	CYS308
D	GLU470
D	SER471
D	HIS472

site_id	AD2
Number of Residues	22
Details	binding site for residue IMP D 501

Chain	Residue
D	ALA49
D	MET51
D	ASN280
D	GLY305
D	SER306
D	ILE307
D	CYS308
D	ASP341
D	GLY343
D	MET362
D	GLY364
D	SER365
D	TYR388
D	GLY390
D	MET391
D	GLY392
D	GLU416
D	GLY417
D	8L4502
D	HOH608
D	HOH618
D	HOH619

site_id	AD3
Number of Residues	12
Details	binding site for residue 8L4 D 502

Chain	Residue
B	PRO27
B	ALA441
B	GLY444
B	TYR445
D	ALA253
D	HIS254
D	THR310
D	MET391
D	GLY392
D	VAL414
D	GLU416
D	IMP501

site_id	AD4
Number of Residues	19
Details	binding site for residue IMP E 501

Chain	Residue
E	ALA49
E	MET51
E	GLY305
E	SER306
E	ILE307
E	CYS308
E	ASP341
E	GLY342
E	GLY343
E	MET362
E	GLY364
E	SER365
E	TYR388
E	GLY390
E	MET391
E	GLY392
E	GLU416
E	GLY417
E	8L4502

site_id	AD5
Number of Residues	11
Details	binding site for residue 8L4 E 502

Chain	Residue
E	ALA253
E	THR310
E	MET391
E	GLY392
E	VAL414
E	GLU416
E	IMP501
G	PRO27
G	ALA441
G	GLY444
G	TYR445

site_id	AD6
Number of Residues	6
Details	binding site for residue K E 503

Chain	Residue
E	GLU470
E	SER471
E	HIS472
F	GLY303
F	GLY305
F	CYS308

site_id	AD7
Number of Residues	6
Details	binding site for residue K E 504

Chain	Residue
E	GLY303
E	GLY305
E	CYS308
G	GLU470
G	SER471
G	HIS472

site_id	AD8
Number of Residues	20
Details	binding site for residue IMP F 500

Chain	Residue
F	ALA49
F	MET51
F	ASN280
F	GLY305
F	SER306
F	ILE307
F	CYS308
F	ASP341
F	GLY342
F	GLY343
F	MET362
F	GLY364
F	SER365
F	TYR388
F	GLY390
F	MET391
F	GLY392
F	GLU416
F	GLY417
F	8L4501

site_id	AD9
Number of Residues	10
Details	binding site for residue 8L4 F 501

Chain	Residue
E	PRO27
E	GLY444
E	TYR445
F	ALA253
F	THR310
F	MET391
F	GLY392
F	VAL414
F	GLU416
F	IMP500

site_id	AE1
Number of Residues	6
Details	binding site for residue K F 502

Chain	Residue
F	GLU470
F	SER471
F	HIS472
H	GLY303
H	GLY305
H	CYS308

site_id	AE2
Number of Residues	20
Details	binding site for residue IMP G 501

Chain	Residue
G	ALA49
G	MET51
G	GLY305
G	SER306
G	ILE307
G	CYS308
G	ASP341
G	GLY342
G	GLY343
G	GLY364
G	SER365
G	TYR388
G	GLY390
G	MET391
G	GLY392
G	GLU416
G	GLY417
G	8L4502
G	HOH601
G	HOH604

site_id	AE3
Number of Residues	11
Details	binding site for residue 8L4 G 502

Chain	Residue
G	ALA253
G	HIS254
G	THR310
G	MET391
G	GLY392
G	GLU416
G	IMP501
H	PRO27
H	ALA441
H	GLY444
H	TYR445

site_id	AE4
Number of Residues	6
Details	binding site for residue K G 503

Chain	Residue
G	GLY303
G	GLY305
G	CYS308
H	GLU470
H	SER471
H	HIS472

site_id	AE5
Number of Residues	16
Details	binding site for residue IMP H 501

Chain	Residue
H	ALA49
H	MET51
H	GLY305
H	SER306
H	ILE307
H	CYS308
H	ASP341
H	GLY343
H	GLY364
H	SER365
H	TYR388
H	GLY390
H	MET391
H	GLY392
H	GLU416
H	8L4502

site_id	AE6
Number of Residues	13
Details	binding site for residue 8L4 H 502

Chain	Residue
F	ALA441
F	GLY444
F	TYR445
H	THR252
H	ALA253
H	HIS254
H	THR310
H	MET391
H	GLY392
H	MET397
H	VAL414
H	GLU416
H	IMP501

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	VAL298-THR310

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