Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4MYX

Crystal Structure of the Inosine 5'-monophosphate Dehydrogenase, with a Internal Deletion of CBS Domain from Bacillus anthracis str. Ame complexed with P32

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	19
Details	BINDING SITE FOR RESIDUE IMP A 501

Chain	Residue
A	ALA49
A	MET362
A	GLY364
A	SER365
A	TYR388
A	GLY390
A	MET391
A	GLY392
A	GLU416
A	2F0502
A	HOH604
A	MET51
A	GLY305
A	SER306
A	ILE307
A	CYS308
A	ASP341
A	GLY342
A	GLY343

site_id	AC2
Number of Residues	11
Details	BINDING SITE FOR RESIDUE 2F0 A 502

Chain	Residue
A	ALA253
A	THR310
A	MET391
A	GLY392
A	VAL414
A	GLU416
A	IMP501
A	HOH645
C	ALA441
C	GLY444
C	TYR445

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FMT A 503

Chain	Residue
A	ARG311
C	LEU17
C	LYS352
C	HIS472

site_id	AC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE FMT A 504

Chain	Residue
A	ILE379
A	GLY382

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL A 505

Chain	Residue
A	VAL476
A	GLN477
A	ILE478

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MLI A 506

Chain	Residue
A	ALA284
A	GLU285
A	LYS288
A	GLU330
A	LYS333

site_id	AC7
Number of Residues	22
Details	BINDING SITE FOR RESIDUE IMP B 500

Chain	Residue
B	ALA49
B	MET51
B	GLY305
B	SER306
B	CYS308
B	ASP341
B	GLY342
B	GLY343
B	LEU363
B	GLY364
B	SER365
B	TYR388
B	GLY390
B	MET391
B	GLY392
B	GLU416
B	GLY417
B	2F0501
B	HOH609
B	HOH613
B	HOH625
B	HOH638

site_id	AC8
Number of Residues	13
Details	BINDING SITE FOR RESIDUE 2F0 B 501

Chain	Residue
A	PRO27
A	ALA441
A	GLY444
A	TYR445
B	THR252
B	ALA253
B	HIS254
B	MET391
B	GLY392
B	MET397
B	VAL414
B	GLU416
B	IMP500

site_id	AC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO B 502

Chain	Residue
A	SER464
B	ARG462
B	MET463

site_id	BC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE FMT B 503

Chain	Residue
B	THR283
B	ALA284
B	ASP326

site_id	BC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE FMT C 501

Chain	Residue
C	MET463
C	HOH610

site_id	BC3
Number of Residues	23
Details	BINDING SITE FOR RESIDUE IMP C 502

Chain	Residue
C	SER365
C	TYR388
C	GLY390
C	MET391
C	GLY392
C	GLU416
C	GLY417
C	2F0503
C	HOH604
C	HOH605
C	HOH620
C	ALA49
C	MET51
C	GLY305
C	SER306
C	ILE307
C	CYS308
C	THR310
C	ASP341
C	GLY342
C	GLY343
C	MET362
C	GLY364

site_id	BC4
Number of Residues	12
Details	BINDING SITE FOR RESIDUE 2F0 C 503

Chain	Residue
C	HIS254
C	THR310
C	MET391
C	GLY392
C	VAL414
C	GLU416
C	IMP502
D	LEU26
D	PRO27
D	ALA441
D	GLY444
D	TYR445

site_id	BC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO C 504

Chain	Residue
C	THR34
C	VAL35
C	HIS359
C	GLU452
C	ARG455

site_id	BC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 C 505

Chain	Residue
C	LYS333
C	HIS334
C	GLY335
C	HOH642

site_id	BC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO C 506

Chain	Residue
C	MET366
C	LYS425
C	THR431
C	GLN434
C	PRO483
C	ASN484

site_id	BC8
Number of Residues	9
Details	BINDING SITE FOR RESIDUE 2F0 D 501

Chain	Residue
B	ALA441
B	GLY444
B	TYR445
D	ALA253
D	THR310
D	MET391
D	MET397
D	GLU416
D	IMP504

site_id	BC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO D 502

Chain	Residue
C	PHE6
C	VAL7
D	ARG462

site_id	CC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO D 503

Chain	Residue
D	LYS425
D	THR431
D	PRO483

site_id	CC2
Number of Residues	21
Details	BINDING SITE FOR RESIDUE IMP D 504

Chain	Residue
D	ALA49
D	MET51
D	ASN280
D	GLY305
D	SER306
D	ILE307
D	CYS308
D	THR310
D	ASP341
D	GLY342
D	GLY343
D	GLY364
D	SER365
D	TYR388
D	GLY390
D	MET391
D	GLY392
D	GLU416
D	GLY417
D	2F0501
D	HOH609

site_id	CC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE EDO D 505

Chain	Residue
D	ASP58
D	GLU372

site_id	CC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE FMT D 506

Chain	Residue
D	SER365
D	MET366
D	ALA368
D	GLY369
D	VAL422
D	PRO423
D	LYS425

site_id	CC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FMT D 507

Chain	Residue
C	MET1
D	ALA21
D	CYS446
D	ASN457
D	ALA458

site_id	CC6
Number of Residues	22
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	2F0502
E	HOH608

site_id	CC7
Number of Residues	9
Details	BINDING SITE FOR RESIDUE 2F0 E 502

Chain	Residue
E	THR310
E	MET391
E	GLY392
E	MET397
E	GLU416
E	IMP501
F	ALA441
F	GLY444
F	TYR445

site_id	CC8
Number of Residues	1
Details	BINDING SITE FOR RESIDUE FMT E 503

Chain	Residue
E	GLU3

site_id	CC9
Number of Residues	2
Details	BINDING SITE FOR RESIDUE EDO E 505

Chain	Residue
E	VAL35
E	HIS359

site_id	DC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL E 506

Chain	Residue
B	PHE-4
E	VAL476
E	GLN477
E	ILE478

site_id	DC2
Number of Residues	1
Details	BINDING SITE FOR RESIDUE FMT E 507

Chain	Residue
E	THR322

site_id	DC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MLI E 508

Chain	Residue
E	ALA284
E	GLU285
E	LYS288
E	GLU330

site_id	DC4
Number of Residues	12
Details	BINDING SITE FOR RESIDUE 2F0 E 509

Chain	Residue
E	PRO27
E	ALA441
E	GLY444
E	TYR445
G	THR252
G	ALA253
G	HIS254
G	THR310
G	MET391
G	GLY392
G	GLU416
G	IMP501

site_id	DC5
Number of Residues	25
Details	BINDING SITE FOR RESIDUE IMP F 501

Chain	Residue
F	ALA49
F	MET51
F	GLY305
F	SER306
F	ILE307
F	CYS308
F	THR310
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	2F0502
F	HOH606
F	HOH607
F	HOH608
F	HOH612
F	HOH613

site_id	DC6
Number of Residues	11
Details	BINDING SITE FOR RESIDUE 2F0 F 502

Chain	Residue
F	ALA253
F	THR310
F	GLY392
F	VAL414
F	GLU416
F	IMP501
H	LEU26
H	PRO27
H	ALA441
H	GLY444
H	TYR445

site_id	DC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE FMT F 503

Chain	Residue
F	THR283
F	ALA284
F	ASP326

site_id	DC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO F 504

Chain	Residue
F	VAL35
F	HIS359
F	ARG455

site_id	DC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO F 506

Chain	Residue
E	ARG311
F	ASP14
F	LEU17
F	LYS352
F	HIS472
F	HOH611

site_id	EC1
Number of Residues	1
Details	BINDING SITE FOR RESIDUE FMT F 507

Chain	Residue
F	ARG332

site_id	EC2
Number of Residues	20
Details	BINDING SITE FOR RESIDUE IMP G 501

Chain	Residue
E	2F0509
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	HOH638
G	HOH639

site_id	EC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 G 502

Chain	Residue
G	VAL19
G	PRO20
G	ALA21
G	GLN459

site_id	EC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 G 503

Chain	Residue
G	GLU38
G	ARG268
G	SER273
G	LEU274
G	ASN275
G	ASN296

site_id	EC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE FMT H 501

Chain	Residue
F	PHE6
H	ARG462

site_id	EC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FMT H 502

Chain	Residue
F	ARG311
H	ASP14
H	LEU17
H	LYS352

site_id	EC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FMT H 503

Chain	Residue
H	TYR325
H	ASP326
H	HOH617
H	HOH618

site_id	EC8
Number of Residues	21
Details	BINDING SITE FOR RESIDUE IMP H 504

Chain	Residue
H	ALA49
H	MET51
H	ASN280
H	GLY305
H	SER306
H	ILE307
H	CYS308
H	THR310
H	ASP341
H	GLY342
H	GLY343
H	MET362
H	GLY364
H	SER365
H	TYR388
H	GLY390
H	MET391
H	GLY392
H	GLU416
H	GLY417
H	2F0505

site_id	EC9
Number of Residues	8
Details	BINDING SITE FOR RESIDUE 2F0 H 505

Chain	Residue
G	ALA441
G	GLY444
G	TYR445
H	ALA253
H	THR310
H	MET391
H	GLU416
H	IMP504

site_id	FC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FMT H 506

Chain	Residue
H	GLN41
H	LEU42
H	ASN43
H	ALA64
H	GLY67
H	GLY68

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)