2F1K
Crystal structure of Synechocystis arogenate dehydrogenase
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0004665 | molecular_function | prephenate dehydrogenase (NADP+) activity |
A | 0006571 | biological_process | tyrosine biosynthetic process |
A | 0008977 | molecular_function | prephenate dehydrogenase (NAD+) activity |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0042802 | molecular_function | identical protein binding |
A | 0070403 | molecular_function | NAD+ binding |
B | 0000166 | molecular_function | nucleotide binding |
B | 0004665 | molecular_function | prephenate dehydrogenase (NADP+) activity |
B | 0006571 | biological_process | tyrosine biosynthetic process |
B | 0008977 | molecular_function | prephenate dehydrogenase (NAD+) activity |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0042802 | molecular_function | identical protein binding |
B | 0070403 | molecular_function | NAD+ binding |
C | 0000166 | molecular_function | nucleotide binding |
C | 0004665 | molecular_function | prephenate dehydrogenase (NADP+) activity |
C | 0006571 | biological_process | tyrosine biosynthetic process |
C | 0008977 | molecular_function | prephenate dehydrogenase (NAD+) activity |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0042802 | molecular_function | identical protein binding |
C | 0070403 | molecular_function | NAD+ binding |
D | 0000166 | molecular_function | nucleotide binding |
D | 0004665 | molecular_function | prephenate dehydrogenase (NADP+) activity |
D | 0006571 | biological_process | tyrosine biosynthetic process |
D | 0008977 | molecular_function | prephenate dehydrogenase (NAD+) activity |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0042802 | molecular_function | identical protein binding |
D | 0070403 | molecular_function | NAD+ binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE TRS C 1001 |
Chain | Residue |
C | ASP197 |
C | ASP199 |
D | ASP169 |
D | HOH4423 |
site_id | AC2 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE TRS D 1002 |
Chain | Residue |
D | GLU127 |
D | ASN128 |
D | LEU129 |
D | HOH4417 |
D | HOH4424 |
B | GLU126 |
B | GLU127 |
B | ASN128 |
B | LEU129 |
D | GLU126 |
site_id | AC3 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE NAP A 1350 |
Chain | Residue |
A | GLY7 |
A | GLY9 |
A | LEU10 |
A | ILE11 |
A | SER30 |
A | ARG31 |
A | GLN32 |
A | THR35 |
A | CYS64 |
A | THR65 |
A | PRO66 |
A | ILE67 |
A | VAL90 |
A | ALA91 |
A | SER92 |
A | PRO113 |
A | ALA115 |
A | GLY116 |
A | THR117 |
A | GLN120 |
A | GLY121 |
A | HOH1352 |
A | HOH1370 |
A | HOH1392 |
site_id | AC4 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE NAP B 2350 |
Chain | Residue |
B | GLY7 |
B | GLY9 |
B | LEU10 |
B | ILE11 |
B | SER30 |
B | ARG31 |
B | GLN32 |
B | THR35 |
B | CYS64 |
B | THR65 |
B | PRO66 |
B | ILE67 |
B | LEU69 |
B | VAL90 |
B | ALA91 |
B | SER92 |
B | PRO113 |
B | ALA115 |
B | GLN120 |
B | GLY121 |
B | HOH2355 |
B | HOH2395 |
B | HOH2450 |
site_id | AC5 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE NAP C 3350 |
Chain | Residue |
C | GLY7 |
C | GLY9 |
C | LEU10 |
C | ILE11 |
C | SER30 |
C | ARG31 |
C | GLN32 |
C | THR35 |
C | CYS64 |
C | THR65 |
C | ILE67 |
C | LEU69 |
C | VAL90 |
C | ALA91 |
C | SER92 |
C | HIS112 |
C | PRO113 |
C | ALA115 |
C | GLY116 |
C | GLN120 |
C | GLY121 |
site_id | AC6 |
Number of Residues | 28 |
Details | BINDING SITE FOR RESIDUE NAP D 4350 |
Chain | Residue |
D | PRO113 |
D | ALA115 |
D | GLY116 |
D | GLN120 |
D | GLY121 |
D | HOH4355 |
D | HOH4369 |
D | HOH4401 |
D | HOH4430 |
D | HOH4470 |
D | HOH4474 |
D | GLY7 |
D | GLY9 |
D | LEU10 |
D | ILE11 |
D | SER30 |
D | ARG31 |
D | GLN32 |
D | THR35 |
D | CYS64 |
D | THR65 |
D | PRO66 |
D | ILE67 |
D | LEU69 |
D | VAL90 |
D | ALA91 |
D | SER92 |
D | HIS112 |