Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5KAH

Crystal structure of a dioxygenase in the Crotonase superfamily in P21, V425T mutant

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
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	0003824	molecular_function	catalytic activity
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	0003824	molecular_function	catalytic activity
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	0003824	molecular_function	catalytic activity
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	0003824	molecular_function	catalytic activity
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	0003824	molecular_function	catalytic activity
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	0003824	molecular_function	catalytic activity
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	0003824	molecular_function	catalytic activity
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	0003824	molecular_function	catalytic activity
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	0003824	molecular_function	catalytic activity
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	0003824	molecular_function	catalytic activity
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	0003824	molecular_function	catalytic activity
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	168
Details	Binding site: {"evidences":[{"source":"PubMed","id":"18004875","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)