Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5URS

Crystal Structure of the Catalytic Domain of the Inosine Monophosphate Dehydrogenase from Bacillus anthracis in the complex with IMP and the inhibitor P178

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	22
Details	binding site for residue IMP A 501

Chain	Residue
A	ALA49
A	GLY343
A	MET362
A	LEU363
A	GLY364
A	SER365
A	TYR388
A	GLY390
A	MET391
A	GLY392
A	GLU416
A	MET51
A	8LA502
A	HOH617
A	HOH628
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 8LA A 502

Chain	Residue
A	THR252
A	ALA253
A	HIS254
A	SER257
A	GLY259
A	THR310
A	GLY392
A	GLU416
A	IMP501
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	3
Details	binding site for residue EDO A 504

Chain	Residue
A	LEU11
A	ARG462
A	MET463

site_id	AC5
Number of Residues	6
Details	binding site for residue K A 505

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

site_id	AC6
Number of Residues	16
Details	binding site for residue IMP B 500

Chain	Residue
B	ALA49
B	GLY305
B	SER306
B	CYS308
B	ASP341
B	GLY342
B	GLY343
B	GLY364
B	SER365
B	TYR388
B	GLY390
B	MET391
B	GLY392
B	GLU416
B	GLY417
B	8LA501

site_id	AC7
Number of Residues	11
Details	binding site for residue 8LA B 501

Chain	Residue
A	GLY444
B	ALA253
B	HIS254
B	SER257
B	GLY259
B	VAL260
B	MET391
B	GLY392
B	GLU416
B	IMP500
B	HOH621

site_id	AC8
Number of Residues	7
Details	binding site for residue K B 502

Chain	Residue
B	GLU470
B	SER471
B	HIS472
D	GLY303
D	PRO304
D	GLY305
D	CYS308

site_id	AC9
Number of Residues	23
Details	binding site for residue IMP C 501

Chain	Residue
C	MET391
C	GLY392
C	GLU416
C	GLY417
C	8LA502
C	HOH613
C	HOH620
C	ALA49
C	MET51
C	ASN280
C	GLY305
C	SER306
C	ILE307
C	CYS308
C	ASP341
C	GLY342
C	GLY343
C	MET362
C	LEU363
C	GLY364
C	SER365
C	TYR388
C	GLY390

site_id	AD1
Number of Residues	15
Details	binding site for residue 8LA C 502

Chain	Residue
C	THR252
C	ALA253
C	HIS254
C	SER257
C	GLY259
C	VAL260
C	MET391
C	GLY392
C	VAL414
C	GLU416
C	IMP501
D	LEU26
D	ALA441
D	GLY444
D	TYR445

site_id	AD2
Number of Residues	4
Details	binding site for residue PO4 C 503

Chain	Residue
C	ARG332
C	GLY357
C	ARG455
C	GLU456

site_id	AD3
Number of Residues	8
Details	binding site for residue PO4 C 504

Chain	Residue
C	ARG311
C	VAL312
C	HOH604
D	ASP14
D	LEU17
D	LYS352
D	LEU468
D	SER471

site_id	AD4
Number of Residues	6
Details	binding site for residue K C 505

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

site_id	AD5
Number of Residues	25
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	GLY342
D	GLY343
D	MET362
D	LEU363
D	GLY364
D	SER365
D	TYR388
D	GLY390
D	MET391
D	GLY392
D	GLU416
D	GLY417
D	8LA502
D	HOH604
D	HOH608
D	HOH612
D	HOH634

site_id	AD6
Number of Residues	16
Details	binding site for residue 8LA D 502

Chain	Residue
B	LEU26
B	ALA441
B	GLY444
D	THR252
D	ALA253
D	HIS254
D	SER257
D	GLY259
D	VAL260
D	THR310
D	MET391
D	GLY392
D	VAL414
D	GLU416
D	IMP501
D	HOH623

site_id	AD7
Number of Residues	3
Details	binding site for residue GOL D 503

Chain	Residue
B	SER464
D	ASP15
D	ARG462

site_id	AD8
Number of Residues	23
Details	binding site for residue IMP E 501

Chain	Residue
E	ALA49
E	MET51
E	ASN280
E	GLY305
E	SER306
E	ILE307
E	CYS308
E	ASP341
E	GLY342
E	GLY343
E	MET362
E	LEU363
E	GLY364
E	SER365
E	TYR388
E	GLY390
E	MET391
E	GLY392
E	GLU416
E	GLY417
E	8LA502
E	HOH604
E	HOH624

site_id	AD9
Number of Residues	17
Details	binding site for residue 8LA E 502

Chain	Residue
E	VAL229
E	THR252
E	ALA253
E	HIS254
E	SER257
E	GLY259
E	VAL260
E	THR310
E	MET391
E	GLY392
E	VAL414
E	GLU416
E	IMP501
E	HOH628
G	ALA441
G	GLY444
G	TYR445

site_id	AE1
Number of Residues	7
Details	binding site for residue K E 503

Chain	Residue
E	GLU470
E	SER471
E	HIS472
F	GLY303
F	PRO304
F	GLY305
F	CYS308

site_id	AE2
Number of Residues	1
Details	binding site for residue PEG E 504

Chain	Residue
E	ASN296

site_id	AE3
Number of Residues	3
Details	binding site for residue PO4 E 505

Chain	Residue
E	THR322
E	ASP326
F	PHE6

site_id	AE4
Number of Residues	6
Details	binding site for residue K E 506

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

site_id	AE5
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	GLY343
F	MET362
F	GLY364
F	SER365
F	TYR388
F	GLY390
F	MET391
F	GLY392
F	GLU416
F	GLY417
F	8LA501
F	HOH607

site_id	AE6
Number of Residues	16
Details	binding site for residue 8LA F 501

Chain	Residue
E	PRO27
E	GLY444
E	TYR445
F	VAL229
F	THR252
F	ALA253
F	HIS254
F	SER257
F	GLY259
F	VAL260
F	THR310
F	MET391
F	GLY392
F	VAL414
F	GLU416
F	IMP500

site_id	AE7
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	AE8
Number of Residues	22
Details	binding site for residue IMP G 500

Chain	Residue
G	ALA49
G	MET51
G	ASN280
G	GLY305
G	SER306
G	ILE307
G	CYS308
G	ASP341
G	GLY342
G	GLY343
G	MET362
G	LEU363
G	GLY364
G	SER365
G	TYR388
G	GLY390
G	MET391
G	GLY392
G	GLU416
G	GLY417
G	8LA501
G	HOH612

site_id	AE9
Number of Residues	14
Details	binding site for residue 8LA G 501

Chain	Residue
G	THR252
G	ALA253
G	HIS254
G	SER257
G	GLY259
G	VAL260
G	MET391
G	GLY392
G	GLU416
G	IMP500
H	LEU26
H	ALA441
H	GLY444
H	TYR445

site_id	AF1
Number of Residues	6
Details	binding site for residue K G 502

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

site_id	AF2
Number of Residues	19
Details	binding site for residue IMP H 500

Chain	Residue
H	ALA49
H	MET51
H	GLY305
H	SER306
H	ILE307
H	CYS308
H	ASP341
H	GLY343
H	MET362
H	LEU363
H	GLY364
H	SER365
H	TYR388
H	GLY390
H	MET391
H	GLY392
H	GLU416
H	GLY417
H	8LA501

site_id	AF3
Number of Residues	15
Details	binding site for residue 8LA H 501

Chain	Residue
F	PRO27
F	ALA441
F	GLY444
F	TYR445
H	VAL229
H	THR252
H	ALA253
H	HIS254
H	SER257
H	GLY259
H	VAL260
H	MET391
H	GLY392
H	GLU416
H	IMP500

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)