6XBC
Crystal structure of Streptomyces sviceus SsDesB
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0006879 | biological_process | intracellular iron ion homeostasis |
A | 0047091 | molecular_function | L-lysine 6-monooxygenase (NADPH) activity |
B | 0000166 | molecular_function | nucleotide binding |
B | 0006879 | biological_process | intracellular iron ion homeostasis |
B | 0047091 | molecular_function | L-lysine 6-monooxygenase (NADPH) activity |
C | 0000166 | molecular_function | nucleotide binding |
C | 0006879 | biological_process | intracellular iron ion homeostasis |
C | 0047091 | molecular_function | L-lysine 6-monooxygenase (NADPH) activity |
D | 0000166 | molecular_function | nucleotide binding |
D | 0006879 | biological_process | intracellular iron ion homeostasis |
D | 0047091 | molecular_function | L-lysine 6-monooxygenase (NADPH) activity |
E | 0000166 | molecular_function | nucleotide binding |
E | 0006879 | biological_process | intracellular iron ion homeostasis |
E | 0047091 | molecular_function | L-lysine 6-monooxygenase (NADPH) activity |
F | 0000166 | molecular_function | nucleotide binding |
F | 0006879 | biological_process | intracellular iron ion homeostasis |
F | 0047091 | molecular_function | L-lysine 6-monooxygenase (NADPH) activity |
G | 0000166 | molecular_function | nucleotide binding |
G | 0006879 | biological_process | intracellular iron ion homeostasis |
G | 0047091 | molecular_function | L-lysine 6-monooxygenase (NADPH) activity |
H | 0000166 | molecular_function | nucleotide binding |
H | 0006879 | biological_process | intracellular iron ion homeostasis |
H | 0047091 | molecular_function | L-lysine 6-monooxygenase (NADPH) activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 23 |
Details | binding site for residue FAD A 501 |
Chain | Residue |
A | GLY18 |
A | LEU60 |
A | GLN61 |
A | THR62 |
A | VAL126 |
A | GLY154 |
A | THR155 |
A | GLY156 |
A | TYR337 |
A | PHE344 |
A | ASN379 |
A | GLY20 |
A | PRO390 |
A | ASP391 |
A | LEU392 |
H | ASN308 |
A | PRO21 |
A | PHE22 |
A | GLU42 |
A | SER43 |
A | LYS44 |
A | TRP49 |
A | HIS50 |
site_id | AC2 |
Number of Residues | 24 |
Details | binding site for residue FAD B 501 |
Chain | Residue |
B | GLY18 |
B | GLY20 |
B | PRO21 |
B | PHE22 |
B | LEU41 |
B | GLU42 |
B | SER43 |
B | LYS44 |
B | TRP49 |
B | HIS50 |
B | LEU60 |
B | GLN61 |
B | THR62 |
B | THR124 |
B | THR125 |
B | VAL126 |
B | GLY154 |
B | THR155 |
B | GLY156 |
B | TYR337 |
B | ASN379 |
B | PRO390 |
B | ASP391 |
B | LEU392 |
site_id | AC3 |
Number of Residues | 23 |
Details | binding site for residue FAD C 501 |
Chain | Residue |
C | GLY18 |
C | GLY20 |
C | PRO21 |
C | PHE22 |
C | LEU41 |
C | GLU42 |
C | SER43 |
C | LYS44 |
C | TRP49 |
C | HIS50 |
C | LEU60 |
C | GLN61 |
C | THR62 |
C | VAL126 |
C | GLY154 |
C | THR155 |
C | GLY156 |
C | TYR337 |
C | PHE344 |
C | ASN379 |
C | PRO390 |
C | ASP391 |
C | LEU392 |
site_id | AC4 |
Number of Residues | 21 |
Details | binding site for residue FAD D 501 |
Chain | Residue |
D | GLY18 |
D | GLY20 |
D | PRO21 |
D | PHE22 |
D | GLU42 |
D | SER43 |
D | LYS44 |
D | TRP49 |
D | HIS50 |
D | GLN61 |
D | THR62 |
D | THR125 |
D | VAL126 |
D | GLY154 |
D | THR155 |
D | GLY156 |
D | TYR337 |
D | ASN379 |
D | PRO390 |
D | ASP391 |
D | LEU392 |
site_id | AC5 |
Number of Residues | 22 |
Details | binding site for residue FAD E 501 |
Chain | Residue |
E | HIS50 |
E | LEU60 |
E | GLN61 |
E | THR62 |
E | VAL126 |
E | GLY154 |
E | THR155 |
E | GLY156 |
E | TYR337 |
E | PHE344 |
E | ASN379 |
E | PRO390 |
E | ASP391 |
E | LEU392 |
E | GLY18 |
E | GLY20 |
E | PRO21 |
E | PHE22 |
E | GLU42 |
E | SER43 |
E | LYS44 |
E | TRP49 |
site_id | AC6 |
Number of Residues | 22 |
Details | binding site for residue FAD F 501 |
Chain | Residue |
F | GLY18 |
F | GLY20 |
F | PRO21 |
F | PHE22 |
F | LEU41 |
F | GLU42 |
F | SER43 |
F | LYS44 |
F | TRP49 |
F | HIS50 |
F | GLN61 |
F | THR62 |
F | THR124 |
F | VAL126 |
F | GLY154 |
F | THR155 |
F | GLY156 |
F | TYR337 |
F | ASN379 |
F | PRO390 |
F | ASP391 |
F | LEU392 |
site_id | AC7 |
Number of Residues | 24 |
Details | binding site for residue FAD G 501 |
Chain | Residue |
G | GLY18 |
G | LEU19 |
G | GLY20 |
G | PRO21 |
G | PHE22 |
G | GLU42 |
G | SER43 |
G | LYS44 |
G | TRP49 |
G | HIS50 |
G | LEU60 |
G | GLN61 |
G | THR62 |
G | ARG103 |
G | VAL126 |
G | GLY154 |
G | THR155 |
G | GLY156 |
G | TYR337 |
G | PHE344 |
G | ASN379 |
G | PRO390 |
G | ASP391 |
G | LEU392 |
site_id | AC8 |
Number of Residues | 24 |
Details | binding site for residue FAD H 501 |
Chain | Residue |
A | ASN308 |
H | GLY18 |
H | GLY20 |
H | PRO21 |
H | PHE22 |
H | LEU41 |
H | GLU42 |
H | SER43 |
H | LYS44 |
H | TRP49 |
H | HIS50 |
H | LEU60 |
H | GLN61 |
H | THR62 |
H | THR124 |
H | VAL126 |
H | GLY154 |
H | THR155 |
H | GLY156 |
H | TYR337 |
H | ASN379 |
H | PRO390 |
H | ASP391 |
H | LEU392 |