4RAP

Crystal structure of bacterial iron-containing dodecameric glycosyltransferase TibC from enterotoxigenic E.coli H10407

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0016757	molecular_function	glycosyltransferase activity
A	0046872	molecular_function	metal ion binding
B	0016757	molecular_function	glycosyltransferase activity
B	0046872	molecular_function	metal ion binding
C	0016757	molecular_function	glycosyltransferase activity
C	0046872	molecular_function	metal ion binding
D	0016757	molecular_function	glycosyltransferase activity
D	0046872	molecular_function	metal ion binding
E	0016757	molecular_function	glycosyltransferase activity
E	0046872	molecular_function	metal ion binding
F	0016757	molecular_function	glycosyltransferase activity
F	0046872	molecular_function	metal ion binding
G	0016757	molecular_function	glycosyltransferase activity
G	0046872	molecular_function	metal ion binding
H	0016757	molecular_function	glycosyltransferase activity
H	0046872	molecular_function	metal ion binding
I	0016757	molecular_function	glycosyltransferase activity
I	0046872	molecular_function	metal ion binding
J	0016757	molecular_function	glycosyltransferase activity
J	0046872	molecular_function	metal ion binding
K	0016757	molecular_function	glycosyltransferase activity
K	0046872	molecular_function	metal ion binding
L	0016757	molecular_function	glycosyltransferase activity
L	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE A 501

Chain	Residue
A	CYS339
A	CYS342
A	CYS358
A	CYS370

---

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE B 501

Chain	Residue
B	CYS339
B	CYS342
B	CYS358
B	CYS370

---

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE C 501

Chain	Residue
C	CYS342
C	CYS358
C	CYS370
C	CYS339

---

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO C 502

Chain	Residue
C	ARG189
C	ARG200
C	GLU201

---

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE D 501

Chain	Residue
D	CYS339
D	CYS342
D	CYS358
D	CYS370

---

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE E 1400

Chain	Residue
E	CYS339
E	CYS342
E	CYS358
E	CYS370

---

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE F 501

Chain	Residue
F	CYS339
F	CYS342
F	CYS358
F	CYS370

---

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE G 1400

Chain	Residue
G	CYS339
G	CYS342
G	CYS358
G	CYS370

---

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE H 501

Chain	Residue
H	CYS339
H	CYS342
H	CYS358
H	CYS370

---

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE I 501

Chain	Residue
I	CYS339
I	CYS342
I	CYS358
I	CYS370

---

site_id	BC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE EDO I 502

Chain	Residue
I	ARG189
I	GLU201

---

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO I 503

Chain	Residue
F	TRP272
I	ALA259
I	HIS260
I	ASP276

---

site_id	BC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE J 501

Chain	Residue
J	CYS339
J	CYS342
J	CYS358
J	CYS370

---

site_id	BC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO J 502

Chain	Residue
J	ARG189
J	ARG200
J	GLU201

---

site_id	BC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE K 501

Chain	Residue
K	CYS339
K	CYS342
K	CYS358
K	CYS370

---

site_id	BC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE FE L 501

Chain	Residue
L	CYS339
L	CYS342
L	CYS358
L	CYS370

---

site_id	BC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE EDO L 502

Chain	Residue
L	ARG189
L	GLU201

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	ACT_SITE: Proton acceptor => ECO:0000269|PubMed:25310236

Chain	Residue	Details
A	ASP110
J	ASP110
K	ASP110
L	ASP110
B	ASP110
C	ASP110
D	ASP110
E	ASP110
F	ASP110
G	ASP110
H	ASP110
I	ASP110

---

site_id	SWS_FT_FI2
Number of Residues	120
Details	BINDING: BINDING => ECO:0000269|PubMed:25310236, ECO:0007744|PDB:4RB4

Chain	Residue	Details
A	THR107
A	GLU326
J	GLU326
K	THR107
K	LEU108
K	GLY109
K	GLN224
K	THR226
K	LYS230
K	ARG257
K	LEU281
K	GLY302
B	THR107
K	GLU326
L	THR107
L	LEU108
L	GLY109
L	GLN224
L	THR226
L	LYS230
L	ARG257
L	LEU281
L	GLY302
B	LEU108
L	GLU326
B	GLY109
B	GLN224
B	THR226
B	LYS230
B	ARG257
B	LEU281
B	GLY302
A	LEU108
B	GLU326
C	THR107
C	LEU108
C	GLY109
C	GLN224
C	THR226
C	LYS230
C	ARG257
C	LEU281
C	GLY302
A	GLY109
C	GLU326
D	THR107
D	LEU108
D	GLY109
D	GLN224
D	THR226
D	LYS230
D	ARG257
D	LEU281
D	GLY302
A	GLN224
D	GLU326
E	THR107
E	LEU108
E	GLY109
E	GLN224
E	THR226
E	LYS230
E	ARG257
E	LEU281
E	GLY302
A	THR226
E	GLU326
F	THR107
F	LEU108
F	GLY109
F	GLN224
F	THR226
F	LYS230
F	ARG257
F	LEU281
F	GLY302
A	LYS230
F	GLU326
G	THR107
G	LEU108
G	GLY109
G	GLN224
G	THR226
G	LYS230
G	ARG257
G	LEU281
G	GLY302
A	ARG257
G	GLU326
H	THR107
H	LEU108
H	GLY109
H	GLN224
H	THR226
H	LYS230
H	ARG257
H	LEU281
H	GLY302
A	LEU281
H	GLU326
I	THR107
I	LEU108
I	GLY109
I	GLN224
I	THR226
I	LYS230
I	ARG257
I	LEU281
I	GLY302
A	GLY302
I	GLU326
J	THR107
J	LEU108
J	GLY109
J	GLN224
J	THR226
J	LYS230
J	ARG257
J	LEU281
J	GLY302

---

site_id	SWS_FT_FI3
Number of Residues	36
Details	BINDING: BINDING => ECO:0000269|PubMed:25310236, ECO:0007744|PDB:4RAP, ECO:0007744|PDB:4RB4

Chain	Residue	Details
A	CYS339
D	CYS339
D	CYS342
D	CYS358
E	CYS339
E	CYS342
E	CYS358
F	CYS339
F	CYS342
F	CYS358
G	CYS339
A	CYS342
G	CYS342
G	CYS358
H	CYS339
H	CYS342
H	CYS358
I	CYS339
I	CYS342
I	CYS358
J	CYS339
J	CYS342
A	CYS358
J	CYS358
K	CYS339
K	CYS342
K	CYS358
L	CYS339
L	CYS342
L	CYS358
B	CYS339
B	CYS342
B	CYS358
C	CYS339
C	CYS342
C	CYS358

---

site_id	SWS_FT_FI4
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269|PubMed:25310236, ECO:0007744|PDB:4RAP

Chain	Residue	Details
A	CYS370
J	CYS370
K	CYS370
L	CYS370
B	CYS370
C	CYS370
D	CYS370
E	CYS370
F	CYS370
G	CYS370
H	CYS370
I	CYS370

---