4MY1

Crystal Structure of the Inosine 5'-monophosphate Dehydrogenase, with a Internal Deletion of CBS Domain from Bacillus anthracis str. Ames complexed with P68

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	16
Details	BINDING SITE FOR RESIDUE IMP A 500

Chain	Residue
A	ALA49
A	TYR388
A	GLY390
A	MET391
A	GLY392
A	GLU416
A	GLY417
A	P68501
A	GLY305
A	SER306
A	CYS308
A	ASP341
A	GLY342
A	GLY343
A	GLY364
A	SER365

---

site_id	AC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE P68 A 501

Chain	Residue
A	THR310
A	GLY392
A	LEU413
A	VAL414
A	GLU416
A	IMP500
A	HOH612
C	ALA441
C	TYR445

---

site_id	AC3
Number of Residues	19
Details	BINDING SITE FOR RESIDUE IMP B 500

Chain	Residue
B	ALA49
B	MET51
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	P68501
B	HOH603

---

site_id	AC4
Number of Residues	11
Details	BINDING SITE FOR RESIDUE P68 B 501

Chain	Residue
A	PRO27
A	GLY444
A	TYR445
B	ALA253
B	THR310
B	MET391
B	GLY392
B	MET397
B	VAL414
B	GLU416
B	IMP500

---

site_id	AC5
Number of Residues	20
Details	BINDING SITE FOR RESIDUE IMP C 500

Chain	Residue
C	ALA49
C	MET51
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
C	MET391
C	GLY392
C	GLU416
C	P68501
C	HOH613

---

site_id	AC6
Number of Residues	12
Details	BINDING SITE FOR RESIDUE P68 C 501

Chain	Residue
C	HIS254
C	THR310
C	MET391
C	GLY392
C	VAL414
C	GLU416
C	IMP500
C	HOH604
C	HOH612
D	ALA441
D	GLY444
D	TYR445

---

site_id	AC7
Number of Residues	19
Details	BINDING SITE FOR RESIDUE IMP D 500

Chain	Residue
D	TYR388
D	GLY390
D	MET391
D	GLY392
D	GLU416
D	GLY417
D	P68501
D	ALA49
D	MET51
D	GLY305
D	SER306
D	ILE307
D	CYS308
D	ASP341
D	GLY342
D	GLY343
D	MET362
D	GLY364
D	SER365

---

site_id	AC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE P68 D 501

Chain	Residue
B	TYR445
D	ALA253
D	MET391
D	GLY392
D	VAL414
D	GLU416
D	IMP500

---

site_id	AC9
Number of Residues	20
Details	BINDING SITE FOR RESIDUE IMP E 501

Chain	Residue
E	ALA49
E	MET51
E	GLY305
E	SER306
E	ILE307
E	CYS308
E	THR310
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	P68502

---

site_id	BC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE P68 E 502

Chain	Residue
E	ALA253
E	HIS254
E	THR310
E	MET391
E	GLY392
E	VAL414
E	GLU416
E	IMP501
G	TYR445

---

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE P68 E 503

Chain	Residue
E	GLY444
E	TYR445
F	THR310
F	GLY392
F	IMP500

---

site_id	BC3
Number of Residues	19
Details	BINDING SITE FOR RESIDUE IMP F 500

Chain	Residue
E	P68503
F	ALA49
F	MET51
F	GLY305
F	SER306
F	ILE307
F	CYS308
F	ASP341
F	GLY343
F	MET362
F	LEU363
F	GLY364
F	SER365
F	TYR388
F	GLY390
F	MET391
F	GLY392
F	GLU416
F	GLY417

---

site_id	BC4
Number of Residues	19
Details	BINDING SITE FOR RESIDUE IMP G 500

Chain	Residue
G	ALA49
G	MET51
G	ASN280
G	GLY305
G	SER306
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	P68501

---

site_id	BC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE P68 G 501

Chain	Residue
G	MET391
G	MET397
G	VAL414
G	GLU416
G	IMP500
H	TYR445

---

site_id	BC6
Number of Residues	18
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	GLY342
H	GLY343
H	GLY364
H	SER365
H	TYR388
H	GLY390
H	MET391
H	GLY392
H	GLU416
H	GLY417
H	P68501

---

site_id	BC7
Number of Residues	9
Details	BINDING SITE FOR RESIDUE P68 H 501

Chain	Residue
F	PRO27
F	GLY444
F	TYR445
H	THR310
H	MET391
H	GLY392
H	MET397
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

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