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Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

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	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	HIS385
B	ASP163
B	GLY212
B	GLU383
B	SER384
B	HIS385
C	ASP163
C	GLY212
C	GLU383
C	SER384
C	HIS385
D	ASP163
D	GLY212
D	GLU383
D	SER384
D	HIS385
A	ASP163
A	GLY212
A	GLU383
A	SER384

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

Chain	Residue	Details
A	GLY214
A	GLY216
A	CYS219
B	GLY214
B	GLY216
B	CYS219
C	GLY214
C	GLY216
C	CYS219
D	GLY214
D	GLY216
D	CYS219

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

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

221051

PDB entries from 2024-06-12

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