4ZAH

Crystal structure of sugar aminotransferase WecE with External Aldimine VII from Escherichia coli K-12

Replaces:  4WFP

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000271	biological_process	polysaccharide biosynthetic process
A	0009246	biological_process	enterobacterial common antigen biosynthetic process
A	0016740	molecular_function	transferase activity
A	0019180	molecular_function	dTDP-4-amino-4,6-dideoxygalactose transaminase activity
A	0030170	molecular_function	pyridoxal phosphate binding
A	0042802	molecular_function	identical protein binding
B	0000271	biological_process	polysaccharide biosynthetic process
B	0009246	biological_process	enterobacterial common antigen biosynthetic process
B	0016740	molecular_function	transferase activity
B	0019180	molecular_function	dTDP-4-amino-4,6-dideoxygalactose transaminase activity
B	0030170	molecular_function	pyridoxal phosphate binding
B	0042802	molecular_function	identical protein binding
C	0000271	biological_process	polysaccharide biosynthetic process
C	0009246	biological_process	enterobacterial common antigen biosynthetic process
C	0016740	molecular_function	transferase activity
C	0019180	molecular_function	dTDP-4-amino-4,6-dideoxygalactose transaminase activity
C	0030170	molecular_function	pyridoxal phosphate binding
C	0042802	molecular_function	identical protein binding
D	0000271	biological_process	polysaccharide biosynthetic process
D	0009246	biological_process	enterobacterial common antigen biosynthetic process
D	0016740	molecular_function	transferase activity
D	0019180	molecular_function	dTDP-4-amino-4,6-dideoxygalactose transaminase activity
D	0030170	molecular_function	pyridoxal phosphate binding
D	0042802	molecular_function	identical protein binding
E	0000271	biological_process	polysaccharide biosynthetic process
E	0009246	biological_process	enterobacterial common antigen biosynthetic process
E	0016740	molecular_function	transferase activity
E	0019180	molecular_function	dTDP-4-amino-4,6-dideoxygalactose transaminase activity
E	0030170	molecular_function	pyridoxal phosphate binding
E	0042802	molecular_function	identical protein binding
F	0000271	biological_process	polysaccharide biosynthetic process
F	0009246	biological_process	enterobacterial common antigen biosynthetic process
F	0016740	molecular_function	transferase activity
F	0019180	molecular_function	dTDP-4-amino-4,6-dideoxygalactose transaminase activity
F	0030170	molecular_function	pyridoxal phosphate binding
F	0042802	molecular_function	identical protein binding
G	0000271	biological_process	polysaccharide biosynthetic process
G	0009246	biological_process	enterobacterial common antigen biosynthetic process
G	0016740	molecular_function	transferase activity
G	0019180	molecular_function	dTDP-4-amino-4,6-dideoxygalactose transaminase activity
G	0030170	molecular_function	pyridoxal phosphate binding
G	0042802	molecular_function	identical protein binding
H	0000271	biological_process	polysaccharide biosynthetic process
H	0009246	biological_process	enterobacterial common antigen biosynthetic process
H	0016740	molecular_function	transferase activity
H	0019180	molecular_function	dTDP-4-amino-4,6-dideoxygalactose transaminase activity
H	0030170	molecular_function	pyridoxal phosphate binding
H	0042802	molecular_function	identical protein binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	31
Details	binding site for residue T5K A 500

Chain	Residue
A	PHE4
A	SER176
A	HIS178
A	THR180
A	LYS181
A	GLY189
A	VAL318
A	PHE319
A	HIS320
A	TYR321
A	ARG352
A	SER54
A	HOH637
A	HOH651
A	HOH670
A	HOH675
A	HOH677
A	HOH683
A	HOH720
A	HOH727
B	ARG213
B	TYR224
A	CYS55
B	HOH623
B	HOH634
A	THR56
A	PHE81
A	VAL126
A	ASP152
A	ALA154
A	GLN155

---

site_id	AC2
Number of Residues	25
Details	binding site for residue T5K B 500

Chain	Residue
A	TYR224
A	HOH641
B	PHE4
B	SER54
B	CYS55
B	THR56
B	PHE81
B	ASP152
B	ALA154
B	GLN155
B	SER176
B	HIS178
B	LYS181
B	GLY189
B	VAL318
B	PHE319
B	HIS320
B	TYR321
B	ILE322
B	ARG352
B	HOH601
B	HOH627
B	HOH639
B	HOH664
B	HOH682

---

site_id	AC3
Number of Residues	26
Details	binding site for residue T5K C 500

Chain	Residue
C	SER54
C	CYS55
C	THR56
C	PHE81
C	VAL126
C	ASP152
C	ALA154
C	GLN155
C	SER176
C	HIS178
C	LYS181
C	GLY189
C	VAL318
C	PHE319
C	HIS320
C	TYR321
C	ILE322
C	ARG352
C	HOH603
C	HOH613
C	HOH628
C	HOH656
C	HOH682
D	ARG213
D	LYS223
D	TYR224

---

site_id	AC4
Number of Residues	21
Details	binding site for residue T5K D 500

Chain	Residue
D	ARG352
D	HOH623
D	HOH632
D	HOH660
C	TYR224
D	PHE4
D	SER54
D	CYS55
D	THR56
D	PHE81
D	VAL126
D	ASP152
D	ALA154
D	GLN155
D	SER176
D	LYS181
D	GLY189
D	VAL318
D	PHE319
D	HIS320
D	TYR321

---

site_id	AC5
Number of Residues	23
Details	binding site for residue T5K E 500

Chain	Residue
E	SER54
E	CYS55
E	THR56
E	THR80
E	PHE81
E	VAL126
E	ASP152
E	ALA154
E	GLN155
E	SER176
E	HIS178
E	LYS181
E	GLY189
E	VAL318
E	PHE319
E	HIS320
E	TYR321
E	ARG352
E	HOH605
E	HOH650
E	HOH671
F	ARG213
F	TYR224

---

site_id	AC6
Number of Residues	23
Details	binding site for residue T5K F 500

Chain	Residue
E	TYR224
F	PHE4
F	SER54
F	CYS55
F	THR56
F	THR80
F	PHE81
F	ASP152
F	ALA154
F	GLN155
F	SER176
F	HIS178
F	THR180
F	LYS181
F	GLY189
F	VAL318
F	PHE319
F	HIS320
F	TYR321
F	ARG352
F	HOH601
F	HOH602
F	HOH606

---

site_id	AC7
Number of Residues	23
Details	binding site for residue T5K G 500

Chain	Residue
G	PHE4
G	SER54
G	CYS55
G	THR56
G	THR80
G	PHE81
G	ASP152
G	ALA154
G	GLN155
G	SER176
G	HIS178
G	THR180
G	LYS181
G	GLY189
G	VAL318
G	PHE319
G	HIS320
G	TYR321
G	ILE322
G	ARG352
G	HOH607
H	ARG213
H	TYR224

---

site_id	AC8
Number of Residues	22
Details	binding site for residue T5K H 500

Chain	Residue
G	TYR224
H	SER54
H	CYS55
H	THR56
H	PHE81
H	VAL126
H	ASP152
H	ALA154
H	GLN155
H	SER176
H	HIS178
H	THR180
H	LYS181
H	GLY189
H	VAL318
H	PHE319
H	HIS320
H	TYR321
H	ILE322
H	ARG352
H	HOH612
H	HOH613

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000250|UniProtKB:Q8ZNF3, ECO:0000255|HAMAP-Rule:MF_02026

Chain	Residue	Details
A	LYS181
B	LYS181
C	LYS181
D	LYS181
E	LYS181
F	LYS181
G	LYS181
H	LYS181

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