Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1PVN

The crystal structure of the complex between IMP dehydrogenase catalytic domain and a transition state analogue MZP

Replaces: 1MWF

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	6
Details	BINDING SITE FOR RESIDUE K A 981

Chain	Residue
A	GLU485
A	GLY486
A	GLY487
D	GLY314
D	GLY316
D	CYS319

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE K B 982

Chain	Residue
B	GLU485
B	GLY486
B	GLY487
A	GLY314
A	GLY316
A	CYS319

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE K D 983

Chain	Residue
C	GLY314
C	GLY316
C	CYS319
D	GLU485
D	GLY486
D	GLY487

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE K C 984

Chain	Residue
C	ASP264
C	PHE266
D	GLY20
D	SER22
D	ASN460

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE K C 985

Chain	Residue
B	GLY314
B	GLY316
B	CYS319
C	GLU485
C	GLY486
C	GLY487

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE K B 986

Chain	Residue
B	ASP264
B	PHE266
C	GLY20
C	SER22
C	ASN460

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE K A 987

Chain	Residue
A	ASP264
A	PHE266
B	GLY20
B	SER22
B	ASN460

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE K A 988

Chain	Residue
A	GLY20
A	SER22
A	ASN460
D	ASP264
D	PHE266

site_id	AC9
Number of Residues	27
Details	BINDING SITE FOR RESIDUE MZP A 971

Chain	Residue
A	ALA57
A	MET59
A	GLY316
A	SER317
A	ILE318
A	CYS319
A	ASP358
A	GLY359
A	GLY360
A	MET379
A	LEU380
A	GLY381
A	ARG382
A	TYR405
A	GLY407
A	GLU408
A	GLY409
A	ARG418
A	TYR419
A	GLU431
A	GLY432
A	HOH1004
A	HOH1010
A	HOH1012
A	HOH1028
A	HOH1029
A	HOH1053

site_id	BC1
Number of Residues	29
Details	BINDING SITE FOR RESIDUE MZP B 972

Chain	Residue
B	HOH1124
B	ALA57
B	MET59
B	GLY316
B	SER317
B	ILE318
B	CYS319
B	ASP358
B	GLY359
B	GLY360
B	MET379
B	LEU380
B	GLY381
B	ARG382
B	TYR405
B	GLY407
B	GLU408
B	GLY409
B	ARG418
B	TYR419
B	GLU431
B	GLY432
B	HOH997
B	HOH1000
B	HOH1008
B	HOH1023
B	HOH1036
B	HOH1041
B	HOH1046

site_id	BC2
Number of Residues	27
Details	BINDING SITE FOR RESIDUE MZP C 973

Chain	Residue
C	ALA57
C	MET59
C	GLY316
C	SER317
C	ILE318
C	CYS319
C	ASP358
C	GLY359
C	GLY360
C	MET379
C	LEU380
C	GLY381
C	ARG382
C	TYR405
C	GLY407
C	GLU408
C	GLY409
C	ARG418
C	TYR419
C	GLU431
C	GLY432
C	HOH998
C	HOH1005
C	HOH1007
C	HOH1014
C	HOH1015
C	HOH1039

site_id	BC3
Number of Residues	27
Details	BINDING SITE FOR RESIDUE MZP D 974

Chain	Residue
D	ALA57
D	MET59
D	GLY316
D	SER317
D	ILE318
D	CYS319
D	ASP358
D	GLY359
D	GLY360
D	MET379
D	LEU380
D	GLY381
D	ARG382
D	TYR405
D	GLY407
D	GLU408
D	GLY409
D	ARG418
D	TYR419
D	GLU431
D	GLY432
D	HOH1001
D	HOH1005
D	HOH1017
D	HOH1022
D	HOH1037
D	HOH1051

site_id	BC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE TRS B 991

Chain	Residue
B	ASP364
B	TYR383
B	ARG386
B	ASN446
B	ALA449
B	SER450
B	LYS453
B	HOH1192

site_id	BC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE TRS C 992

Chain	Residue
B	ALA2
C	VAL339
C	ASN343
C	HOH997
C	HOH999
C	HOH1051
C	HOH1063

site_id	BC6
Number of Residues	9
Details	BINDING SITE FOR RESIDUE TRS A 993

Chain	Residue
A	VAL339
A	ALA340
A	ASN343
A	HOH1001
A	HOH1018
A	HOH1040
A	HOH1093
A	HOH1097
D	ALA2

site_id	BC7
Number of Residues	9
Details	BINDING SITE FOR RESIDUE TRS B 994

Chain	Residue
A	ALA2
A	HOH1008
B	VAL339
B	ASN343
B	HOH999
B	HOH1075
B	HOH1077
B	HOH1176
B	HOH1233

site_id	BC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE TRS D 995

Chain	Residue
C	ALA2
C	HOH1040
D	VAL339
D	ASN343
D	HOH998
D	HOH1011
D	HOH1085

site_id	BC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE TRS A 996

Chain	Residue
A	TYR15
A	ILE336
A	LEU477
A	HOH1062
D	HOH999
D	HOH1069
D	HOH1084

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ILE309-THR321

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Thioimidate intermediate","evidences":[{"source":"HAMAP-Rule","id":"MF_03156","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12235158","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12549902","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	4
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_03156","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	24
Details	Binding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"12549902","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details