Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6PXA

The crystal structure of chloramphenicol acetyltransferase-like protein from Vibrio fischeri ES114 in complex with taurocholic acid

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0008811	molecular_function	chloramphenicol O-acetyltransferase activity
A	0016740	molecular_function	transferase activity
A	0016746	molecular_function	acyltransferase activity
A	0046677	biological_process	response to antibiotic
A	0046872	molecular_function	metal ion binding
B	0008811	molecular_function	chloramphenicol O-acetyltransferase activity
B	0016740	molecular_function	transferase activity
B	0016746	molecular_function	acyltransferase activity
B	0046677	biological_process	response to antibiotic
B	0046872	molecular_function	metal ion binding
C	0008811	molecular_function	chloramphenicol O-acetyltransferase activity
C	0016740	molecular_function	transferase activity
C	0016746	molecular_function	acyltransferase activity
C	0046677	biological_process	response to antibiotic
C	0046872	molecular_function	metal ion binding
D	0008811	molecular_function	chloramphenicol O-acetyltransferase activity
D	0016740	molecular_function	transferase activity
D	0016746	molecular_function	acyltransferase activity
D	0046677	biological_process	response to antibiotic
D	0046872	molecular_function	metal ion binding
E	0008811	molecular_function	chloramphenicol O-acetyltransferase activity
E	0016740	molecular_function	transferase activity
E	0016746	molecular_function	acyltransferase activity
E	0046677	biological_process	response to antibiotic
E	0046872	molecular_function	metal ion binding
F	0008811	molecular_function	chloramphenicol O-acetyltransferase activity
F	0016740	molecular_function	transferase activity
F	0016746	molecular_function	acyltransferase activity
F	0046677	biological_process	response to antibiotic
F	0046872	molecular_function	metal ion binding
G	0008811	molecular_function	chloramphenicol O-acetyltransferase activity
G	0016740	molecular_function	transferase activity
G	0016746	molecular_function	acyltransferase activity
G	0046677	biological_process	response to antibiotic
G	0046872	molecular_function	metal ion binding
H	0008811	molecular_function	chloramphenicol O-acetyltransferase activity
H	0016740	molecular_function	transferase activity
H	0016746	molecular_function	acyltransferase activity
H	0046677	biological_process	response to antibiotic
H	0046872	molecular_function	metal ion binding
I	0008811	molecular_function	chloramphenicol O-acetyltransferase activity
I	0016740	molecular_function	transferase activity
I	0016746	molecular_function	acyltransferase activity
I	0046677	biological_process	response to antibiotic
I	0046872	molecular_function	metal ion binding
J	0008811	molecular_function	chloramphenicol O-acetyltransferase activity
J	0016740	molecular_function	transferase activity
J	0016746	molecular_function	acyltransferase activity
J	0046677	biological_process	response to antibiotic
J	0046872	molecular_function	metal ion binding
K	0008811	molecular_function	chloramphenicol O-acetyltransferase activity
K	0016740	molecular_function	transferase activity
K	0016746	molecular_function	acyltransferase activity
K	0046677	biological_process	response to antibiotic
K	0046872	molecular_function	metal ion binding
L	0008811	molecular_function	chloramphenicol O-acetyltransferase activity
L	0016740	molecular_function	transferase activity
L	0016746	molecular_function	acyltransferase activity
L	0046677	biological_process	response to antibiotic
L	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	14
Details	binding site for residue TCH A 301

Chain	Residue
A	PHE62
B	LEU8
B	GLU9
B	GLY10
B	TYR27
B	TYR29
A	GLN88
A	PHE98
A	PRO99
A	PHE100
A	SER101
A	PHE105
A	ACT304
B	TRP7

site_id	AC2
Number of Residues	3
Details	binding site for residue CL A 302

Chain	Residue
A	TYR29
A	SER31
C	HIS90

site_id	AC3
Number of Residues	8
Details	binding site for residue SO4 A 303

Chain	Residue
A	GLU130
A	ARG148
A	HOH408
A	HOH439
B	GLU130
B	ARG148
C	GLU130
C	ARG148

site_id	AC4
Number of Residues	2
Details	binding site for residue ACT A 304

Chain	Residue
A	PRO99
A	TCH301

site_id	AC5
Number of Residues	4
Details	binding site for residue ACT A 305

Chain	Residue
A	HIS138
A	GLY140
A	VAL155
A	ALA156

site_id	AC6
Number of Residues	15
Details	binding site for residue TCH B 301

Chain	Residue
B	PHE62
B	GLN88
B	PHE98
B	PRO99
B	PHE100
B	SER101
B	PHE105
B	GOL303
B	HOH432
C	LEU8
C	GLU9
C	GLY10
C	TYR27
C	TYR29
C	SER31

site_id	AC7
Number of Residues	4
Details	binding site for residue CL B 302

Chain	Residue
A	HIS90
B	TYR29
B	SER31
B	TRP126

site_id	AC8
Number of Residues	2
Details	binding site for residue GOL B 303

Chain	Residue
B	PRO99
B	TCH301

site_id	AC9
Number of Residues	17
Details	binding site for residue TCH C 301

Chain	Residue
A	TRP7
A	LEU8
A	GLU9
A	GLY10
A	TYR27
A	TYR29
A	SER31
A	HOH401
C	PHE62
C	GLN88
C	PHE98
C	PRO99
C	PHE100
C	SER101
C	GLU104
C	PHE105
C	GOL303

site_id	AD1
Number of Residues	4
Details	binding site for residue CL C 302

Chain	Residue
B	HIS90
B	HOH407
C	TYR29
C	SER31

site_id	AD2
Number of Residues	4
Details	binding site for residue GOL C 303

Chain	Residue
C	PRO99
C	PHE100
C	TCH301
C	HOH412

site_id	AD3
Number of Residues	13
Details	binding site for residue TCH D 301

Chain	Residue
D	PHE62
D	GLN88
D	PHE98
D	PRO99
D	PHE100
D	SER101
D	GLU104
D	PHE105
E	LEU8
E	GLU9
E	GLY10
E	TYR27
E	TYR29

site_id	AD4
Number of Residues	3
Details	binding site for residue CL D 302

Chain	Residue
D	TYR29
D	SER31
F	HIS90

site_id	AD5
Number of Residues	2
Details	binding site for residue GOL D 303

Chain	Residue
D	PRO99
D	PHE100

site_id	AD6
Number of Residues	17
Details	binding site for residue TCH E 301

Chain	Residue
E	PHE100
E	SER101
E	GLU104
E	PHE105
E	GOL303
E	HOH414
F	TRP7
F	LEU8
F	GLU9
F	GLY10
F	TYR27
F	TYR29
F	SER31
E	PHE62
E	GLN88
E	PHE98
E	PRO99

site_id	AD7
Number of Residues	4
Details	binding site for residue CL E 302

Chain	Residue
D	HIS90
D	HOH411
E	TYR29
E	SER31

site_id	AD8
Number of Residues	3
Details	binding site for residue GOL E 303

Chain	Residue
E	PRO99
E	PHE100
E	TCH301

site_id	AD9
Number of Residues	16
Details	binding site for residue TCH F 301

Chain	Residue
D	TRP7
D	LEU8
D	GLU9
D	GLY10
D	TYR27
D	TYR29
D	HOH435
F	PHE62
F	GLN88
F	PHE98
F	PRO99
F	PHE100
F	SER101
F	GLU104
F	PHE105
F	GOL304

site_id	AE1
Number of Residues	4
Details	binding site for residue CL F 302

Chain	Residue
E	HIS90
E	HOH402
F	TYR29
F	SER31

site_id	AE2
Number of Residues	1
Details	binding site for residue CL F 303

Chain	Residue
F	GLU130

site_id	AE3
Number of Residues	2
Details	binding site for residue GOL F 304

Chain	Residue
F	PRO99
F	TCH301

site_id	AE4
Number of Residues	16
Details	binding site for residue TCH G 301

Chain	Residue
G	PHE62
G	GLN88
G	PHE98
G	PRO99
G	PHE100
G	SER101
G	GLU104
G	PHE105
G	ACT306
H	TRP7
H	LEU8
H	GLU9
H	GLY10
H	TYR27
H	TYR29
H	SER31

site_id	AE5
Number of Residues	3
Details	binding site for residue CL G 302

Chain	Residue
G	TYR29
G	SER31
I	HIS90

site_id	AE6
Number of Residues	2
Details	binding site for residue CL G 303

Chain	Residue
G	HIS90
H	TYR29

site_id	AE7
Number of Residues	1
Details	binding site for residue CL G 304

Chain	Residue
G	TRP188

site_id	AE8
Number of Residues	6
Details	binding site for residue SO4 G 305

Chain	Residue
G	GLU130
G	ARG148
H	GLU130
H	ARG148
I	GLU130
I	ARG148

site_id	AE9
Number of Residues	2
Details	binding site for residue ACT G 306

Chain	Residue
G	PRO99
G	TCH301

site_id	AF1
Number of Residues	16
Details	binding site for residue TCH H 301

Chain	Residue
H	PHE62
H	GLN88
H	PHE98
H	PRO99
H	PHE100
H	SER101
H	GLU104
H	PHE105
H	GOL302
H	HOH419
H	HOH457
I	LEU8
I	GLU9
I	GLY10
I	TYR27
I	TYR29

site_id	AF2
Number of Residues	4
Details	binding site for residue GOL H 302

Chain	Residue
H	PRO99
H	PHE100
H	SER101
H	TCH301

site_id	AF3
Number of Residues	16
Details	binding site for residue TCH I 301

Chain	Residue
G	TRP7
G	LEU8
G	GLU9
G	GLY10
G	TYR27
G	TYR29
G	HOH425
I	PHE62
I	GLN88
I	PHE98
I	PRO99
I	PHE100
I	SER101
I	PHE105
I	GOL303
I	HOH401

site_id	AF4
Number of Residues	3
Details	binding site for residue CL I 302

Chain	Residue
H	HIS90
I	TYR29
I	SER31

site_id	AF5
Number of Residues	2
Details	binding site for residue GOL I 303

Chain	Residue
I	PRO99
I	TCH301

site_id	AF6
Number of Residues	15
Details	binding site for residue TCH J 301

Chain	Residue
J	PHE62
J	GLN88
J	PHE98
J	PRO99
J	PHE100
J	SER101
J	PHE105
J	FMT309
K	TRP7
K	LEU8
K	GLU9
K	GLY10
K	TYR27
K	TYR29
K	HOH406

site_id	AF7
Number of Residues	3
Details	binding site for residue CL J 302

Chain	Residue
J	TYR29
J	SER31
L	HIS90

site_id	AF8
Number of Residues	2
Details	binding site for residue CL J 303

Chain	Residue
B	ARG69
J	GLU207

site_id	AF9
Number of Residues	5
Details	binding site for residue SO4 J 304

Chain	Residue
J	GLU198
J	ILE199
J	HIS204
J	GLU207
L	LYS110

site_id	AG1
Number of Residues	7
Details	binding site for residue SO4 J 305

Chain	Residue
J	GLU130
J	ARG148
J	HOH411
K	GLU130
K	ARG148
L	GLU130
L	ARG148

site_id	AG2
Number of Residues	2
Details	binding site for residue FMT J 306

Chain	Residue
J	ASP26
J	TRP188

site_id	AG3
Number of Residues	6
Details	binding site for residue FMT J 307

Chain	Residue
J	ASN154
J	VAL155
J	ASN165
J	VAL167
J	HOH404
J	HOH440

site_id	AG4
Number of Residues	1
Details	binding site for residue FMT J 308

Chain	Residue
J	GLU209

site_id	AG5
Number of Residues	2
Details	binding site for residue FMT J 309

Chain	Residue
J	PRO99
J	TCH301

site_id	AG6
Number of Residues	16
Details	binding site for residue TCH K 301

Chain	Residue
K	PHE62
K	GLN88
K	PHE98
K	PRO99
K	PHE100
K	SER101
K	GLU104
K	PHE105
K	FMT304
K	HOH425
L	TRP7
L	LEU8
L	GLU9
L	GLY10
L	TYR27
L	TYR29

site_id	AG7
Number of Residues	3
Details	binding site for residue CL K 302

Chain	Residue
J	HIS90
K	TYR29
K	SER31

site_id	AG8
Number of Residues	3
Details	binding site for residue FMT K 303

Chain	Residue
K	ASP26
K	LYS72
K	TRP188

site_id	AG9
Number of Residues	3
Details	binding site for residue FMT K 304

Chain	Residue
K	PRO99
K	PHE100
K	TCH301

site_id	AH1
Number of Residues	4
Details	binding site for residue FMT K 305

Chain	Residue
K	VAL150
K	ASN164
L	GLY163
L	CL303

site_id	AH2
Number of Residues	15
Details	binding site for residue TCH L 301

Chain	Residue
J	TRP7
J	LEU8
J	GLU9
J	GLY10
J	TYR27
J	TYR29
L	PHE62
L	GLN88
L	PHE98
L	PRO99
L	PHE100
L	SER101
L	PHE105
L	HOH409
L	HOH414

site_id	AH3
Number of Residues	3
Details	binding site for residue CL L 302

Chain	Residue
K	HIS90
L	TYR29
L	SER31

site_id	AH4
Number of Residues	2
Details	binding site for residue CL L 303

Chain	Residue
K	FMT305
L	HOH451

Functional Information from PROSITE/UniProt

site_id	PS00101
Number of Residues	29
Details	HEXAPEP_TRANSFERASES Hexapeptide-repeat containing-transferases signature. IGseAmImpgVhIGdgAiIGarAvItknV

Chain	Residue	Details
A	ILE127-VAL155

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