4RV8

Co-Crystal Structure of the Catalytic Domain of the Inosine Monophosphate Dehydrogenase from Cryptosporidium parvum and the inhibitor p131

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 500

Chain	Residue
A	SER48
A	MET273
A	GLY275
A	SER276
A	TYR299
A	GLY301
A	MET302
A	GLY303
A	GLU329
A	GLY330
A	I13501
A	MET50
A	HOH604
A	HOH624
A	HOH626
A	HOH635
A	GLY216
A	SER217
A	ILE218
A	OCS219
A	ASP252
A	GLY253
A	GLY254

---

site_id	AC2
Number of Residues	19
Details	BINDING SITE FOR RESIDUE I13 A 501

Chain	Residue
A	SER164
A	ALA165
A	ASN191
A	GLY212
A	THR221
A	MET302
A	GLY303
A	MET308
A	VAL327
A	GLU329
A	IMP500
A	HOH612
A	HOH627
A	HOH647
A	HOH685
D	LEU25
D	SER354
D	GLY357
D	TYR358

---

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL A 502

Chain	Residue
A	ASN38
A	ASP158
A	ILE185
A	ASP186

---

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PEG A 503

Chain	Residue
A	MET326
A	VAL327
A	HOH695
D	PRO26

---

site_id	AC5
Number of Residues	24
Details	BINDING SITE FOR RESIDUE IMP B 501

Chain	Residue
B	SER48
B	MET50
B	GLY216
B	SER217
B	ILE218
B	OCS219
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	I13502
B	HOH605
B	HOH609
B	HOH613
B	HOH620
B	HOH673

---

site_id	AC6
Number of Residues	18
Details	BINDING SITE FOR RESIDUE I13 B 502

Chain	Residue
A	LEU25
A	SER354
A	GLY357
A	TYR358
B	SER164
B	ALA165
B	ASN191
B	GLY212
B	THR221
B	MET302
B	GLY303
B	MET308
B	VAL327
B	GLU329
B	IMP501
B	HOH629
B	HOH652
B	HOH668

---

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL B 503

Chain	Residue
B	VAL157
B	ASP158
B	ILE185
B	ASP186

---

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PEG B 504

Chain	Residue
A	PRO26
B	MET326
B	VAL327

---

site_id	AC9
Number of Residues	15
Details	BINDING SITE FOR RESIDUE I13 B 505

Chain	Residue
B	SER354
B	GLY357
B	TYR358
B	HOH607
C	ALA165
C	ASN191
C	GLY212
C	THR221
C	MET302
C	MET308
C	VAL327
C	GLU329
C	IMP501
C	HOH674
C	HOH675

---

site_id	BC1
Number of Residues	24
Details	BINDING SITE FOR RESIDUE IMP C 501

Chain	Residue
B	I13505
C	SER48
C	MET50
C	GLY216
C	SER217
C	ILE218
C	OCS219
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	HOH603
C	HOH606
C	HOH607
C	HOH624
C	HOH625

---

site_id	BC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL C 502

Chain	Residue
C	ASP158
C	ILE185
C	ASP186

---

site_id	BC3
Number of Residues	17
Details	BINDING SITE FOR RESIDUE I13 C 503

Chain	Residue
C	SER354
C	GLY357
C	TYR358
C	HOH666
C	HOH672
D	HIS166
D	ASN191
D	GLY212
D	THR221
D	MET302
D	GLY303
D	MET308
D	VAL327
D	GLU329
D	IMP501
D	HOH618
D	HOH631

---

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

Chain	Residue
C	I13503
D	SER48
D	MET50
D	ASN191
D	GLY216
D	SER217
D	ILE218
D	OCS219
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	HOH605
D	HOH613
D	HOH628

---

site_id	BC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL D 502

Chain	Residue
D	ASN20
D	LYS370
D	HOH676

---

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	ACT_SITE: Thioimidate intermediate => ECO:0000250|UniProtKB:P50097

Chain	Residue	Details
A	OCS219
B	OCS219
C	OCS219
D	OCS219

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	ACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P9WKI7

Chain	Residue	Details
A	ARG315
B	ARG315
C	ARG315
D	ARG315

---

site_id	SWS_FT_FI3
Number of Residues	20
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P50097

Chain	Residue	Details
A	ASP163
B	HIS385
C	ASP163
C	GLY212
C	GLU383
C	SER384
C	HIS385
D	ASP163
D	GLY212
D	GLU383
D	SER384
A	GLY212
D	HIS385
A	GLU383
A	SER384
A	HIS385
B	ASP163
B	GLY212
B	GLU383
B	SER384

---

site_id	SWS_FT_FI4
Number of Residues	12
Details	BINDING: in other chain => ECO:0000250|UniProtKB:P50097

Chain	Residue	Details
A	GLY214
D	GLY214
D	GLY216
D	OCS219
A	GLY216
A	OCS219
B	GLY214
B	GLY216
B	OCS219
C	GLY214
C	GLY216
C	OCS219

---

site_id	SWS_FT_FI5
Number of Residues	20
Details	BINDING: BINDING => ECO:0000269|PubMed:23668331

Chain	Residue	Details
A	SER217
B	GLU329
C	SER217
C	ASP252
C	GLY275
C	TYR299
C	GLU329
D	SER217
D	ASP252
D	GLY275
D	TYR299
A	ASP252
D	GLU329
A	GLY275
A	TYR299
A	GLU329
B	SER217
B	ASP252
B	GLY275
B	TYR299

---