5KAH
Crystal structure of a dioxygenase in the Crotonase superfamily in P21, V425T mutant
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0006635 | biological_process | fatty acid beta-oxidation |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
A | 0017000 | biological_process | antibiotic biosynthetic process |
A | 0042802 | molecular_function | identical protein binding |
B | 0006635 | biological_process | fatty acid beta-oxidation |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
B | 0017000 | biological_process | antibiotic biosynthetic process |
B | 0042802 | molecular_function | identical protein binding |
C | 0006635 | biological_process | fatty acid beta-oxidation |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
C | 0017000 | biological_process | antibiotic biosynthetic process |
C | 0042802 | molecular_function | identical protein binding |
D | 0006635 | biological_process | fatty acid beta-oxidation |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
D | 0017000 | biological_process | antibiotic biosynthetic process |
D | 0042802 | molecular_function | identical protein binding |
E | 0006635 | biological_process | fatty acid beta-oxidation |
E | 0016491 | molecular_function | oxidoreductase activity |
E | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
E | 0017000 | biological_process | antibiotic biosynthetic process |
E | 0042802 | molecular_function | identical protein binding |
F | 0006635 | biological_process | fatty acid beta-oxidation |
F | 0016491 | molecular_function | oxidoreductase activity |
F | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
F | 0017000 | biological_process | antibiotic biosynthetic process |
F | 0042802 | molecular_function | identical protein binding |
G | 0006635 | biological_process | fatty acid beta-oxidation |
G | 0016491 | molecular_function | oxidoreductase activity |
G | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
G | 0017000 | biological_process | antibiotic biosynthetic process |
G | 0042802 | molecular_function | identical protein binding |
H | 0006635 | biological_process | fatty acid beta-oxidation |
H | 0016491 | molecular_function | oxidoreductase activity |
H | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
H | 0017000 | biological_process | antibiotic biosynthetic process |
H | 0042802 | molecular_function | identical protein binding |
I | 0006635 | biological_process | fatty acid beta-oxidation |
I | 0016491 | molecular_function | oxidoreductase activity |
I | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
I | 0017000 | biological_process | antibiotic biosynthetic process |
I | 0042802 | molecular_function | identical protein binding |
J | 0006635 | biological_process | fatty acid beta-oxidation |
J | 0016491 | molecular_function | oxidoreductase activity |
J | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
J | 0017000 | biological_process | antibiotic biosynthetic process |
J | 0042802 | molecular_function | identical protein binding |
K | 0006635 | biological_process | fatty acid beta-oxidation |
K | 0016491 | molecular_function | oxidoreductase activity |
K | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
K | 0017000 | biological_process | antibiotic biosynthetic process |
K | 0042802 | molecular_function | identical protein binding |
L | 0006635 | biological_process | fatty acid beta-oxidation |
L | 0016491 | molecular_function | oxidoreductase activity |
L | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
L | 0017000 | biological_process | antibiotic biosynthetic process |
L | 0042802 | molecular_function | identical protein binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 28 |
Details | binding site for residue YE1 A 501 |
Chain | Residue |
A | ALA188 |
A | LEU237 |
A | LYS238 |
A | PHE250 |
A | ARG254 |
A | PHE292 |
A | ILE294 |
A | GLY295 |
A | GLY296 |
A | GLN299 |
A | TYR314 |
A | GLU189 |
A | ALA319 |
A | GLU322 |
A | ILE324 |
A | ILE325 |
A | GLY327 |
A | PHE412 |
A | GLN416 |
A | PHE432 |
A | HOH620 |
A | HIS222 |
A | ARG224 |
A | TYR225 |
A | ALA233 |
A | GLY234 |
A | ILE235 |
A | ASN236 |
site_id | AC2 |
Number of Residues | 23 |
Details | binding site for residue YE1 B 501 |
Chain | Residue |
B | ARG185 |
B | LEU186 |
B | ALA188 |
B | GLU189 |
B | HIS222 |
B | ARG224 |
B | TYR225 |
B | ALA233 |
B | GLY234 |
B | ILE235 |
B | ASN236 |
B | LEU237 |
B | LYS238 |
B | PHE250 |
B | ARG254 |
B | PHE292 |
B | GLY295 |
B | GLY296 |
B | PRO318 |
B | ILE324 |
B | ILE325 |
B | GLY327 |
B | GLN416 |
site_id | AC3 |
Number of Residues | 25 |
Details | binding site for residue YE1 C 501 |
Chain | Residue |
C | ARG185 |
C | LEU186 |
C | ALA188 |
C | GLU189 |
C | HIS222 |
C | ARG224 |
C | TYR225 |
C | ALA233 |
C | GLY234 |
C | ILE235 |
C | ASN236 |
C | LEU237 |
C | LYS238 |
C | PHE250 |
C | ARG254 |
C | PHE292 |
C | GLY295 |
C | GLY296 |
C | TYR314 |
C | ILE324 |
C | ILE325 |
C | GLY327 |
C | GLN416 |
C | PHE432 |
C | HOH621 |
site_id | AC4 |
Number of Residues | 25 |
Details | binding site for residue YE1 D 501 |
Chain | Residue |
D | PHE432 |
D | HOH638 |
D | ARG185 |
D | LEU186 |
D | ALA188 |
D | GLU189 |
D | HIS222 |
D | ARG224 |
D | TYR225 |
D | ALA233 |
D | GLY234 |
D | ILE235 |
D | ASN236 |
D | LEU237 |
D | LYS238 |
D | PHE250 |
D | ARG254 |
D | GLU255 |
D | ILE294 |
D | GLY295 |
D | GLY296 |
D | GLN299 |
D | PRO318 |
D | GLY327 |
D | GLN416 |
site_id | AC5 |
Number of Residues | 29 |
Details | binding site for residue YE1 E 501 |
Chain | Residue |
E | ARG185 |
E | LEU186 |
E | ALA188 |
E | GLU189 |
E | HIS222 |
E | ARG224 |
E | TYR225 |
E | ALA233 |
E | GLY234 |
E | ILE235 |
E | ASN236 |
E | LEU237 |
E | LYS238 |
E | PHE250 |
E | ARG254 |
E | PHE292 |
E | ILE294 |
E | GLY295 |
E | GLY296 |
E | TYR314 |
E | PRO318 |
E | GLU322 |
E | ILE324 |
E | ILE325 |
E | GLY327 |
E | GLN416 |
E | PHE432 |
E | HOH629 |
E | HOH653 |
site_id | AC6 |
Number of Residues | 27 |
Details | binding site for residue YE1 F 501 |
Chain | Residue |
F | LEU186 |
F | ALA188 |
F | GLU189 |
F | HIS222 |
F | ARG224 |
F | TYR225 |
F | ALA233 |
F | ILE235 |
F | ASN236 |
F | LEU237 |
F | LYS238 |
F | PHE250 |
F | LEU251 |
F | ARG254 |
F | PHE292 |
F | ILE294 |
F | GLY295 |
F | GLY296 |
F | GLN299 |
F | ALA319 |
F | GLU322 |
F | ILE324 |
F | ILE325 |
F | GLY327 |
F | GLN416 |
F | PHE432 |
I | LYS228 |
site_id | AC7 |
Number of Residues | 26 |
Details | binding site for residue YE1 G 501 |
Chain | Residue |
G | ARG185 |
G | LEU186 |
G | ALA188 |
G | GLU189 |
G | HIS222 |
G | ARG224 |
G | TYR225 |
G | ALA233 |
G | GLY234 |
G | ILE235 |
G | ASN236 |
G | LEU237 |
G | LYS238 |
G | PHE250 |
G | ARG254 |
G | PHE292 |
G | ILE294 |
G | GLY295 |
G | GLY296 |
G | GLN299 |
G | TYR314 |
G | ILE325 |
G | GLY327 |
G | PHE412 |
G | GLN416 |
G | HOH637 |
site_id | AC8 |
Number of Residues | 28 |
Details | binding site for residue YE1 H 501 |
Chain | Residue |
H | LEU186 |
H | ALA188 |
H | GLU189 |
H | HIS222 |
H | ARG224 |
H | TYR225 |
H | ALA233 |
H | GLY234 |
H | ILE235 |
H | ASN236 |
H | LEU237 |
H | LYS238 |
H | LEU251 |
H | ARG254 |
H | PHE292 |
H | ILE294 |
H | GLY296 |
H | GLN299 |
H | TYR314 |
H | PRO318 |
H | ILE324 |
H | ILE325 |
H | GLY327 |
H | GLN416 |
H | PHE432 |
H | HOH605 |
H | HOH622 |
H | HOH630 |
site_id | AC9 |
Number of Residues | 23 |
Details | binding site for residue YE1 I 501 |
Chain | Residue |
F | LYS228 |
I | ALA188 |
I | GLU189 |
I | HIS222 |
I | ARG224 |
I | TYR225 |
I | ALA233 |
I | GLY234 |
I | ILE235 |
I | ASN236 |
I | LEU237 |
I | LYS238 |
I | PHE250 |
I | ARG254 |
I | ILE294 |
I | GLY295 |
I | GLY296 |
I | PRO318 |
I | ALA319 |
I | ILE325 |
I | GLY327 |
I | GLN416 |
I | PHE432 |
site_id | AD1 |
Number of Residues | 27 |
Details | binding site for residue YE1 J 501 |
Chain | Residue |
J | LEU186 |
J | ALA188 |
J | GLU189 |
J | HIS222 |
J | ARG224 |
J | TYR225 |
J | ALA233 |
J | GLY234 |
J | ILE235 |
J | ASN236 |
J | LEU237 |
J | LYS238 |
J | PHE250 |
J | LEU251 |
J | ARG254 |
J | PHE292 |
J | ILE294 |
J | GLY295 |
J | GLY296 |
J | TYR314 |
J | PRO318 |
J | ILE324 |
J | ILE325 |
J | GLY327 |
J | GLN416 |
J | PHE432 |
J | HOH636 |
site_id | AD2 |
Number of Residues | 25 |
Details | binding site for residue YE1 K 501 |
Chain | Residue |
K | ARG185 |
K | ALA188 |
K | GLU189 |
K | HIS222 |
K | ARG224 |
K | TYR225 |
K | ALA233 |
K | GLY234 |
K | ILE235 |
K | ASN236 |
K | LEU237 |
K | LYS238 |
K | PHE250 |
K | LEU251 |
K | ARG254 |
K | ILE294 |
K | GLY296 |
K | GLN299 |
K | ILE324 |
K | ILE325 |
K | GLY327 |
K | GLN416 |
K | PHE432 |
K | HOH618 |
K | HOH653 |
site_id | AD3 |
Number of Residues | 24 |
Details | binding site for residue YE1 L 501 |
Chain | Residue |
L | GLU189 |
L | HIS222 |
L | ARG224 |
L | TYR225 |
L | ALA233 |
L | GLY234 |
L | ILE235 |
L | ASN236 |
L | LEU237 |
L | LYS238 |
L | ARG254 |
L | ILE294 |
L | GLY295 |
L | GLY296 |
L | GLN299 |
L | PRO318 |
L | ILE324 |
L | ILE325 |
L | PRO326 |
L | GLY327 |
L | GLN416 |
L | PHE432 |
L | HOH615 |
L | HOH629 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 84 |
Details | BINDING: BINDING => ECO:0000269|PubMed:18004875 |
Chain | Residue | Details |
A | ASP183 | |
B | HIS222 | |
B | ALA233 | |
B | GLY296 | |
B | ILE325 | |
B | GLN416 | |
C | ASP183 | |
C | GLU189 | |
C | HIS222 | |
C | ALA233 | |
C | GLY296 | |
A | GLU189 | |
C | ILE325 | |
C | GLN416 | |
D | ASP183 | |
D | GLU189 | |
D | HIS222 | |
D | ALA233 | |
D | GLY296 | |
D | ILE325 | |
D | GLN416 | |
E | ASP183 | |
A | HIS222 | |
E | GLU189 | |
E | HIS222 | |
E | ALA233 | |
E | GLY296 | |
E | ILE325 | |
E | GLN416 | |
F | ASP183 | |
F | GLU189 | |
F | HIS222 | |
F | ALA233 | |
A | ALA233 | |
F | GLY296 | |
F | ILE325 | |
F | GLN416 | |
G | ASP183 | |
G | GLU189 | |
G | HIS222 | |
G | ALA233 | |
G | GLY296 | |
G | ILE325 | |
G | GLN416 | |
A | GLY296 | |
H | ASP183 | |
H | GLU189 | |
H | HIS222 | |
H | ALA233 | |
H | GLY296 | |
H | ILE325 | |
H | GLN416 | |
I | ASP183 | |
I | GLU189 | |
I | HIS222 | |
A | ILE325 | |
I | ALA233 | |
I | GLY296 | |
I | ILE325 | |
I | GLN416 | |
J | ASP183 | |
J | GLU189 | |
J | HIS222 | |
J | ALA233 | |
J | GLY296 | |
J | ILE325 | |
A | GLN416 | |
J | GLN416 | |
K | ASP183 | |
K | GLU189 | |
K | HIS222 | |
K | ALA233 | |
K | GLY296 | |
K | ILE325 | |
K | GLN416 | |
L | ASP183 | |
L | GLU189 | |
B | ASP183 | |
L | HIS222 | |
L | ALA233 | |
L | GLY296 | |
L | ILE325 | |
L | GLN416 | |
B | GLU189 |