Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4QJ1

Co-crystal structure of the catalytic domain of the inosine monophosphate dehydrogenase from Cryptosporidium parvum with inhibitor N109

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0003938	molecular_function	IMP dehydrogenase activity
A	0005737	cellular_component	cytoplasm
A	0006164	biological_process	purine nucleotide biosynthetic process
A	0006177	biological_process	GMP biosynthetic process
A	0006183	biological_process	GTP biosynthetic process
A	0016491	molecular_function	oxidoreductase activity
A	0046872	molecular_function	metal ion binding
B	0003824	molecular_function	catalytic activity
B	0003938	molecular_function	IMP dehydrogenase activity
B	0005737	cellular_component	cytoplasm
B	0006164	biological_process	purine nucleotide biosynthetic process
B	0006177	biological_process	GMP biosynthetic process
B	0006183	biological_process	GTP biosynthetic process
B	0016491	molecular_function	oxidoreductase activity
B	0046872	molecular_function	metal ion binding
C	0003824	molecular_function	catalytic activity
C	0003938	molecular_function	IMP dehydrogenase activity
C	0005737	cellular_component	cytoplasm
C	0006164	biological_process	purine nucleotide biosynthetic process
C	0006177	biological_process	GMP biosynthetic process
C	0006183	biological_process	GTP biosynthetic process
C	0016491	molecular_function	oxidoreductase activity
C	0046872	molecular_function	metal ion binding
D	0003824	molecular_function	catalytic activity
D	0003938	molecular_function	IMP dehydrogenase activity
D	0005737	cellular_component	cytoplasm
D	0006164	biological_process	purine nucleotide biosynthetic process
D	0006177	biological_process	GMP biosynthetic process
D	0006183	biological_process	GTP biosynthetic process
D	0016491	molecular_function	oxidoreductase activity
D	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	22
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	N09502
A	MET50
A	HOH601
A	HOH605
A	HOH632
A	ASN191
A	GLY216
A	SER217
A	ILE218
A	CYS219
A	ASP252
A	GLY254

site_id	AC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE N09 A 502

Chain	Residue
A	ALA165
A	HIS166
A	THR221
A	MET302
A	GLY303
A	GLU329
A	IMP501
D	SER354
D	GLY357
D	TYR358

site_id	AC3
Number of Residues	22
Details	BINDING SITE FOR RESIDUE IMP B 501

Chain	Residue
B	SER48
B	MET50
B	ASN191
B	GLY216
B	SER217
B	ILE218
B	CYS219
B	ASP252
B	GLY254
B	MET273
B	GLY275
B	SER276
B	TYR299
B	GLY301
B	MET302
B	GLY303
B	GLU329
B	GLY330
B	N09502
B	HOH611
B	HOH616
B	HOH628

site_id	AC4
Number of Residues	11
Details	BINDING SITE FOR RESIDUE N09 B 502

Chain	Residue
A	SER354
A	GLY357
A	TYR358
B	SER164
B	ALA165
B	HIS166
B	THR221
B	MET302
B	GLY303
B	GLU329
B	IMP501

site_id	AC5
Number of Residues	9
Details	BINDING SITE FOR RESIDUE N09 B 503

Chain	Residue
B	SER354
B	GLY357
B	TYR358
C	ALA165
C	HIS166
C	MET302
C	GLY303
C	GLU329
C	IMP501

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ACY B 504

Chain	Residue
B	GLU375
B	ILE376
C	LYS8

site_id	AC7
Number of Residues	23
Details	BINDING SITE FOR RESIDUE IMP C 501

Chain	Residue
C	HOH614
B	N09503
C	SER48
C	MET50
C	ASN191
C	GLY216
C	SER217
C	ILE218
C	CYS219
C	ASP252
C	GLY253
C	GLY254
C	MET273
C	ILE274
C	GLY275
C	SER276
C	TYR299
C	GLY301
C	MET302
C	GLY303
C	GLU329
C	GLY330
C	HOH604

site_id	AC8
Number of Residues	8
Details	BINDING SITE FOR RESIDUE EDO C 502

Chain	Residue
C	THR377
C	THR378
C	SER379
D	GLU13
D	ASP14
D	ILE376
D	THR377
D	THR378

site_id	AC9
Number of Residues	22
Details	BINDING SITE FOR RESIDUE IMP D 501

Chain	Residue
D	SER48
D	MET50
D	ASN191
D	GLY216
D	SER217
D	ILE218
D	CYS219
D	ASP252
D	GLY254
D	MET273
D	GLY275
D	SER276
D	TYR299
D	GLY301
D	MET302
D	GLY303
D	GLU329
D	GLY330
D	N09502
D	HOH605
D	HOH623
D	HOH624

site_id	BC1
Number of Residues	10
Details	BINDING SITE FOR RESIDUE N09 D 502

Chain	Residue
C	LEU25
C	SER354
C	GLY357
C	TYR358
D	ALA165
D	HIS166
D	MET302
D	GLY303
D	GLU329
D	IMP501

site_id	BC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO D 503

Chain	Residue
D	ILE277
D	LYS338
D	MET396
D	ASN397

site_id	BC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE FMT D 504

Chain	Residue
D	ARG256
D	ILE277
D	SER399

site_id	BC4
Number of Residues	1
Details	BINDING SITE FOR RESIDUE EDO D 505

Chain	Residue
D	LYS8

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	CYS219
B	CYS219
C	CYS219
D	CYS219

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	CYS219
A	GLY216
A	CYS219
B	GLY214
B	GLY216
B	CYS219
C	GLY214
C	GLY216
C	CYS219

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

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)