Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2AZN

X-RAY Structure of 2,5-diamino-6-ribosylamino-4(3h)-pyrimidinone 5-phosphate reductase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0008703	molecular_function	5-amino-6-(5-phosphoribosylamino)uracil reductase activity
A	0009231	biological_process	riboflavin biosynthetic process
A	0016491	molecular_function	oxidoreductase activity
A	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A	0046983	molecular_function	protein dimerization activity
A	0050661	molecular_function	NADP binding
A	0051287	molecular_function	NAD binding
B	0008703	molecular_function	5-amino-6-(5-phosphoribosylamino)uracil reductase activity
B	0009231	biological_process	riboflavin biosynthetic process
B	0016491	molecular_function	oxidoreductase activity
B	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B	0046983	molecular_function	protein dimerization activity
B	0050661	molecular_function	NADP binding
B	0051287	molecular_function	NAD binding
C	0008703	molecular_function	5-amino-6-(5-phosphoribosylamino)uracil reductase activity
C	0009231	biological_process	riboflavin biosynthetic process
C	0016491	molecular_function	oxidoreductase activity
C	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
C	0046983	molecular_function	protein dimerization activity
C	0050661	molecular_function	NADP binding
C	0051287	molecular_function	NAD binding
D	0008703	molecular_function	5-amino-6-(5-phosphoribosylamino)uracil reductase activity
D	0009231	biological_process	riboflavin biosynthetic process
D	0016491	molecular_function	oxidoreductase activity
D	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
D	0046983	molecular_function	protein dimerization activity
D	0050661	molecular_function	NADP binding
D	0051287	molecular_function	NAD binding
E	0008703	molecular_function	5-amino-6-(5-phosphoribosylamino)uracil reductase activity
E	0009231	biological_process	riboflavin biosynthetic process
E	0016491	molecular_function	oxidoreductase activity
E	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
E	0046983	molecular_function	protein dimerization activity
E	0050661	molecular_function	NADP binding
E	0051287	molecular_function	NAD binding
F	0008703	molecular_function	5-amino-6-(5-phosphoribosylamino)uracil reductase activity
F	0009231	biological_process	riboflavin biosynthetic process
F	0016491	molecular_function	oxidoreductase activity
F	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
F	0046983	molecular_function	protein dimerization activity
F	0050661	molecular_function	NADP binding
F	0051287	molecular_function	NAD binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE MA5 D 1001

Chain	Residue
D	GLU113
D	LYS114
D	LYS117
D	ILE118
E	GLU110
E	GLU111
E	LYS114
E	ILE118

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MA5 B 1002

Chain	Residue
B	ASN90
C	LEU89
B	LEU89

site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE MA5 C 1003

Chain	Residue
C	ASN208
C	PHE209
C	TYR210
C	HOH2051
D	ARG211
E	LYS207
E	ASN208
E	HOH2007

site_id	AC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MA5 A 1004

Chain	Residue
A	GLU110
A	LYS114

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MA5 F 1005

Chain	Residue
F	ASN208
F	PHE209
F	TYR210

site_id	AC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MA5 C 1006

Chain	Residue
C	TYR10
C	ILE12
C	SER150
C	GLU171
C	HOH2046
E	ASN47
E	SER150

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MA5 B 1007

Chain	Residue
B	GLU113
B	LYS114
B	LYS117
C	GLU111
C	LYS114
C	ILE118

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MA5 F 1008

Chain	Residue
E	ASN90
F	LEU89
F	ASN90
F	HOH3020

site_id	AC9
Number of Residues	24
Details	BINDING SITE FOR RESIDUE NAP A 2001

Chain	Residue
A	VAL15
A	GLY16
A	LEU23
A	ASN28
A	GLY54
A	ILE55
A	GLY56
A	THR57
A	LYS60
A	ASP61
A	VAL81
A	SER83
A	LYS84
A	ARG86
A	LYS133
A	VAL134
A	LEU136
A	GLU154
A	GLY155
A	GLY156
A	GLY157
A	THR158
A	LEU159
A	HOH2027

site_id	BC1
Number of Residues	25
Details	BINDING SITE FOR RESIDUE NAP B 2002

Chain	Residue
B	VAL15
B	GLY16
B	LEU23
B	ASN28
B	GLY54
B	ILE55
B	GLY56
B	THR57
B	LYS60
B	ASP61
B	VAL81
B	ASP82
B	SER83
B	LYS84
B	ARG86
B	LYS133
B	VAL134
B	GLU154
B	GLY155
B	GLY156
B	GLY157
B	THR158
B	LEU159
B	HOH3031
B	HOH3035

site_id	BC2
Number of Residues	22
Details	BINDING SITE FOR RESIDUE NAP C 2003

Chain	Residue
C	ASP61
C	VAL81
C	SER83
C	ARG86
C	LYS133
C	VAL134
C	GLU154
C	GLY155
C	GLY156
C	GLY157
C	THR158
C	LEU159
C	HOH2021
C	VAL15
C	GLY16
C	LEU23
C	ASN28
C	GLY54
C	ILE55
C	GLY56
C	THR57
C	LYS60

site_id	BC3
Number of Residues	24
Details	BINDING SITE FOR RESIDUE NAP D 2004

Chain	Residue
D	VAL15
D	GLY16
D	LEU23
D	ASN28
D	GLY54
D	ILE55
D	GLY56
D	THR57
D	LYS60
D	ASP61
D	VAL81
D	ASP82
D	SER83
D	LYS84
D	ARG86
D	VAL134
D	LEU136
D	GLU154
D	GLY155
D	GLY156
D	GLY157
D	THR158
D	LEU159
D	HOH2044

site_id	BC4
Number of Residues	26
Details	BINDING SITE FOR RESIDUE NAP E 2005

Chain	Residue
E	VAL15
E	GLY16
E	LEU23
E	ASN28
E	GLY54
E	ILE55
E	GLY56
E	THR57
E	LYS60
E	ASP61
E	VAL81
E	ASP82
E	SER83
E	LYS84
E	ARG86
E	LYS133
E	VAL134
E	LEU136
E	GLU154
E	GLY155
E	GLY156
E	GLY157
E	THR158
E	LEU159
E	HOH2020
E	HOH2043

site_id	BC5
Number of Residues	20
Details	BINDING SITE FOR RESIDUE NAP F 2006

Chain	Residue
F	VAL15
F	GLY16
F	LEU23
F	ASN28
F	GLY54
F	ILE55
F	GLY56
F	THR57
F	ASP61
F	VAL81
F	SER83
F	ARG86
F	VAL134
F	GLU154
F	GLY155
F	GLY156
F	GLY157
F	THR158
F	LEU159
F	HOH3016

site_id	BC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EPE B 3001

Chain	Residue
A	LYS114
A	LYS117
A	ILE118
B	GLU111
B	LYS114
B	LYS115
B	ILE118

site_id	BC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EPE F 3002

Chain	Residue
E	LYS117
F	GLU111
F	LYS114

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	60
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16730025","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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