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 | 36 |
Details | BINDING: BINDING => ECO:0000269|PubMed:16730025 |
Chain | Residue | Details |
C | GLY16 | |
C | THR57 | |
C | ASP61 | |
C | SER83 | |
C | VAL134 | |
C | GLY156 | |
D | GLY16 | |
D | THR57 | |
D | ASP61 | |
D | SER83 | |
D | VAL134 | |
D | GLY156 | |
E | GLY16 | |
E | THR57 | |
E | ASP61 | |
E | SER83 | |
E | VAL134 | |
E | GLY156 | |
F | GLY16 | |
F | THR57 | |
F | ASP61 | |
F | SER83 | |
F | VAL134 | |
F | GLY156 | |
A | GLY16 | |
A | THR57 | |
A | ASP61 | |
A | SER83 | |
A | VAL134 | |
A | GLY156 | |
B | GLY16 | |
B | THR57 | |
B | ASP61 | |
B | SER83 | |
B | VAL134 | |
B | GLY156 |