4IXH

Crystal Structure of the Catalytic Domain of the Inosine Monophosphate Dehydrogenase from Cryptosporidium parvum

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	23
Details	BINDING SITE FOR RESIDUE IMP A 501

Chain	Residue
A	SER48
A	MET273
A	GLY275
A	SER276
A	TYR299
A	GLY301
A	MET302
A	GLY303
A	GLU329
A	GLY330
A	HOH604
A	MET50
A	HOH608
A	HOH609
A	HOH628
B	Q21501
A	GLY216
A	SER217
A	ILE218
A	CYS219
A	ASP252
A	GLY253
A	GLY254

---

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO A 502

Chain	Residue
A	THR33
A	LYS34
A	SER270

---

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO A 503

Chain	Residue
A	VAL224
A	VAL327
A	PRO328
A	HOH646
A	HOH659
B	GLN347

---

site_id	AC4
Number of Residues	15
Details	BINDING SITE FOR RESIDUE Q21 A 504

Chain	Residue
A	SER22
A	VAL24
A	LEU25
A	PRO26
A	SER354
A	TYR358
A	HOH706
D	ALA165
D	SER169
D	THR221
D	MET302
D	GLY303
D	MET308
D	GLU329
D	IMP501

---

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO A 505

Chain	Residue
A	GLN347
A	HOH656
D	VAL224
D	VAL327
D	PRO328
D	HOH646

---

site_id	AC6
Number of Residues	15
Details	BINDING SITE FOR RESIDUE Q21 B 501

Chain	Residue
A	ALA165
A	SER169
A	ASN171
A	THR221
A	MET302
A	GLY303
A	VAL327
A	GLU329
A	IMP501
B	SER22
B	VAL24
B	LEU25
B	SER354
B	TYR358
B	HOH638

---

site_id	AC7
Number of Residues	23
Details	BINDING SITE FOR RESIDUE IMP B 502

Chain	Residue
B	SER48
B	MET50
B	GLY216
B	SER217
B	ILE218
B	CYS219
B	ASP252
B	GLY253
B	GLY254
B	MET273
B	GLY275
B	SER276
B	TYR299
B	GLY301
B	MET302
B	GLY303
B	GLU329
B	GLY330
B	Q21503
B	HOH602
B	HOH608
B	HOH614
B	HOH639

---

site_id	AC8
Number of Residues	16
Details	BINDING SITE FOR RESIDUE Q21 B 503

Chain	Residue
B	IMP502
B	HOH659
C	SER22
C	VAL24
C	LEU25
C	PRO26
C	SER354
C	TYR358
B	ALA165
B	SER169
B	ASN171
B	THR221
B	MET302
B	GLY303
B	VAL327
B	GLU329

---

site_id	AC9
Number of Residues	23
Details	BINDING SITE FOR RESIDUE IMP C 501

Chain	Residue
C	SER48
C	MET50
C	GLY216
C	SER217
C	ILE218
C	CYS219
C	ASP252
C	GLY253
C	GLY254
C	MET273
C	GLY275
C	SER276
C	TYR299
C	GLY301
C	MET302
C	GLY303
C	GLU329
C	GLY330
C	Q21502
C	HOH601
C	HOH605
C	HOH620
C	HOH622

---

site_id	BC1
Number of Residues	16
Details	BINDING SITE FOR RESIDUE Q21 C 502

Chain	Residue
C	ALA165
C	SER169
C	THR221
C	MET302
C	GLY303
C	VAL327
C	GLU329
C	IMP501
C	HOH630
C	HOH712
D	SER22
D	VAL24
D	LEU25
D	PRO26
D	SER354
D	TYR358

---

site_id	BC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO C 503

Chain	Residue
C	SER239
C	SER243
C	GLY268
C	TRP368
C	HOH642
C	HOH664

---

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO C 504

Chain	Residue
C	THR33
C	LYS34
C	SER270
C	TRP368

---

site_id	BC4
Number of Residues	23
Details	BINDING SITE FOR RESIDUE IMP D 501

Chain	Residue
A	Q21504
D	SER48
D	MET50
D	GLY216
D	SER217
D	ILE218
D	CYS219
D	ASP252
D	GLY253
D	GLY254
D	MET273
D	GLY275
D	SER276
D	TYR299
D	GLY301
D	MET302
D	GLY303
D	GLU329
D	GLY330
D	HOH606
D	HOH609
D	HOH611
D	HOH612

---

Functional Information from PROSITE/UniProt

site_id	PS00487
Number of Residues	13
Details	IMP_DH_GMP_RED IMP dehydrogenase / GMP reductase signature. IKVGIGpGSICtT

Chain	Residue	Details
A	ILE209-THR221

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Thioimidate intermediate","evidences":[{"source":"UniProtKB","id":"P50097","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	24
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P50097","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	12
Details	Binding site: {"description":"in other chain","evidences":[{"source":"UniProtKB","id":"P50097","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	36
Details	Binding site: {"evidences":[{"source":"PubMed","id":"23668331","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---