4IRN
Crystal Structure of the Prolyl Acyl Carrier Protein Oxidase AnaB
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
B | 0000166 | molecular_function | nucleotide binding |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
C | 0000166 | molecular_function | nucleotide binding |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
C | 0050660 | molecular_function | flavin adenine dinucleotide binding |
D | 0000166 | molecular_function | nucleotide binding |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
D | 0050660 | molecular_function | flavin adenine dinucleotide binding |
E | 0000166 | molecular_function | nucleotide binding |
E | 0016491 | molecular_function | oxidoreductase activity |
E | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
E | 0050660 | molecular_function | flavin adenine dinucleotide binding |
F | 0000166 | molecular_function | nucleotide binding |
F | 0016491 | molecular_function | oxidoreductase activity |
F | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
F | 0050660 | molecular_function | flavin adenine dinucleotide binding |
G | 0000166 | molecular_function | nucleotide binding |
G | 0016491 | molecular_function | oxidoreductase activity |
G | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
G | 0050660 | molecular_function | flavin adenine dinucleotide binding |
H | 0000166 | molecular_function | nucleotide binding |
H | 0016491 | molecular_function | oxidoreductase activity |
H | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
H | 0050660 | molecular_function | flavin adenine dinucleotide binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE FAD A 400 |
Chain | Residue |
A | PHE87 |
A | THR367 |
A | GLU369 |
A | HOH507 |
A | HOH556 |
B | HIS270 |
B | GLN272 |
B | PHE273 |
B | ILE277 |
B | PHE280 |
B | VAL283 |
A | HIS125 |
B | GLU338 |
B | ILE339 |
B | GLY341 |
B | ALA342 |
D | GLN281 |
A | ALA127 |
A | THR128 |
A | GLY133 |
A | SER134 |
A | TYR158 |
A | THR160 |
A | PHE363 |
site_id | AC2 |
Number of Residues | 26 |
Details | BINDING SITE FOR RESIDUE FAD B 400 |
Chain | Residue |
A | HIS270 |
A | GLN272 |
A | PHE273 |
A | ILE277 |
A | PHE280 |
A | VAL283 |
A | GLU338 |
A | ILE339 |
A | GLY341 |
A | ALA342 |
A | HOH504 |
B | PHE87 |
B | HIS125 |
B | ALA127 |
B | THR128 |
B | GLY133 |
B | SER134 |
B | TYR158 |
B | THR160 |
B | PHE363 |
B | THR367 |
B | GLU369 |
B | VAL373 |
B | HOH517 |
B | HOH556 |
C | GLN281 |
site_id | AC3 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE FAD C 400 |
Chain | Residue |
B | GLN281 |
C | PHE87 |
C | HIS125 |
C | ALA127 |
C | THR128 |
C | GLY133 |
C | SER134 |
C | TYR158 |
C | THR160 |
C | PHE363 |
C | THR367 |
C | GLU369 |
C | HOH505 |
C | HOH560 |
C | HOH569 |
D | HIS270 |
D | PHE273 |
D | ILE277 |
D | PHE280 |
D | VAL283 |
D | GLU338 |
D | ILE339 |
D | GLY341 |
D | ALA342 |
site_id | AC4 |
Number of Residues | 27 |
Details | BINDING SITE FOR RESIDUE FAD D 400 |
Chain | Residue |
D | HOH555 |
D | HOH556 |
A | GLN281 |
C | HIS270 |
C | GLN272 |
C | PHE273 |
C | ILE277 |
C | PHE280 |
C | VAL283 |
C | GLU338 |
C | ILE339 |
C | GLY341 |
C | ALA342 |
C | HOH573 |
D | PHE87 |
D | HIS125 |
D | ALA127 |
D | THR128 |
D | GLY133 |
D | SER134 |
D | TYR158 |
D | THR160 |
D | PHE363 |
D | THR367 |
D | GLU369 |
D | HOH503 |
D | HOH504 |
site_id | AC5 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE FAD E 400 |
Chain | Residue |
E | PHE87 |
E | HIS125 |
E | ALA127 |
E | THR128 |
E | GLY133 |
E | SER134 |
E | TYR158 |
E | THR160 |
E | PHE363 |
E | THR367 |
E | GLU369 |
F | HIS270 |
F | GLN272 |
F | PHE273 |
F | ILE277 |
F | PHE280 |
F | VAL283 |
F | GLU338 |
F | ILE339 |
F | GLY341 |
F | ALA342 |
F | HOH541 |
H | GLN281 |
site_id | AC6 |
Number of Residues | 26 |
Details | BINDING SITE FOR RESIDUE FAD F 400 |
Chain | Residue |
E | HIS270 |
E | GLN272 |
E | PHE273 |
E | ILE277 |
E | PHE280 |
E | VAL283 |
E | GLU338 |
E | ILE339 |
E | GLY341 |
E | ALA342 |
E | HOH534 |
F | PHE87 |
F | HIS125 |
F | ALA127 |
F | THR128 |
F | GLY133 |
F | SER134 |
F | TYR158 |
F | THR160 |
F | PHE363 |
F | THR367 |
F | GLU369 |
F | VAL373 |
F | HOH538 |
F | HOH547 |
G | GLN281 |
site_id | AC7 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE FAD G 400 |
Chain | Residue |
F | GLN281 |
G | PHE87 |
G | HIS125 |
G | ALA127 |
G | THR128 |
G | GLY133 |
G | SER134 |
G | TYR158 |
G | THR160 |
G | PHE363 |
G | THR367 |
G | GLU369 |
G | HOH503 |
G | HOH544 |
H | HIS270 |
H | GLN272 |
H | PHE273 |
H | ILE277 |
H | PHE280 |
H | VAL283 |
H | GLU338 |
H | ILE339 |
H | GLY341 |
H | ALA342 |
site_id | AC8 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE FAD H 400 |
Chain | Residue |
E | GLN281 |
G | HIS270 |
G | GLN272 |
G | PHE273 |
G | ILE277 |
G | PHE280 |
G | VAL283 |
G | GLU338 |
G | ILE339 |
G | GLY341 |
G | ALA342 |
H | PHE87 |
H | HIS125 |
H | ALA127 |
H | THR128 |
H | GLY133 |
H | SER134 |
H | TYR158 |
H | THR160 |
H | PHE363 |
H | THR367 |
H | GLU369 |
H | HOH542 |