5G2Q

The crystal structure of a S-selective transaminase from Arthrobacter sp. with alanine bound

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005829	cellular_component	cytosol
A	0008483	molecular_function	transaminase activity
A	0030170	molecular_function	pyridoxal phosphate binding
B	0005829	cellular_component	cytosol
B	0008483	molecular_function	transaminase activity
B	0030170	molecular_function	pyridoxal phosphate binding
C	0005829	cellular_component	cytosol
C	0008483	molecular_function	transaminase activity
C	0030170	molecular_function	pyridoxal phosphate binding
D	0005829	cellular_component	cytosol
D	0008483	molecular_function	transaminase activity
D	0030170	molecular_function	pyridoxal phosphate binding
E	0005829	cellular_component	cytosol
E	0008483	molecular_function	transaminase activity
E	0030170	molecular_function	pyridoxal phosphate binding
F	0005829	cellular_component	cytosol
F	0008483	molecular_function	transaminase activity
F	0030170	molecular_function	pyridoxal phosphate binding
G	0005829	cellular_component	cytosol
G	0008483	molecular_function	transaminase activity
G	0030170	molecular_function	pyridoxal phosphate binding
H	0005829	cellular_component	cytosol
H	0008483	molecular_function	transaminase activity
H	0030170	molecular_function	pyridoxal phosphate binding
I	0005829	cellular_component	cytosol
I	0008483	molecular_function	transaminase activity
I	0030170	molecular_function	pyridoxal phosphate binding
J	0005829	cellular_component	cytosol
J	0008483	molecular_function	transaminase activity
J	0030170	molecular_function	pyridoxal phosphate binding
K	0005829	cellular_component	cytosol
K	0008483	molecular_function	transaminase activity
K	0030170	molecular_function	pyridoxal phosphate binding
L	0005829	cellular_component	cytosol
L	0008483	molecular_function	transaminase activity
L	0030170	molecular_function	pyridoxal phosphate binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	20
Details	BINDING SITE FOR RESIDUE PDA A 1000

Chain	Residue
A	LEU59
A	VAL271
A	LYS298
A	ARG442
A	HOH2067
A	HOH2082
A	HOH2115
A	HOH2123
A	HOH2161
B	VAL328
B	SER329
A	GLY121
B	THR330
A	SER122
A	TYR148
A	HIS149
A	GLY150
A	GLU237
A	VAL242
A	ASP269

---

site_id	AC2
Number of Residues	18
Details	BINDING SITE FOR RESIDUE PDA B 1000

Chain	Residue
A	VAL328
A	SER329
A	THR330
A	HOH2068
A	HOH2134
A	HOH2135
B	LEU59
B	GLY121
B	SER122
B	TYR148
B	HIS149
B	GLU237
B	VAL242
B	ASP269
B	VAL271
B	LEU272
B	LYS298
B	ARG442

---

site_id	AC3
Number of Residues	18
Details	BINDING SITE FOR RESIDUE PDA C 1000

Chain	Residue
C	LEU59
C	GLY121
C	SER122
C	TYR148
C	HIS149
C	GLY150
C	GLU237
C	VAL242
C	ASP269
C	VAL271
C	LEU272
C	LYS298
C	ARG442
C	HOH2029
C	HOH2042
D	VAL328
D	SER329
D	THR330

---

site_id	AC4
Number of Residues	19
Details	BINDING SITE FOR RESIDUE PDA D 1000

Chain	Residue
C	VAL328
C	THR330
C	HOH2030
C	HOH2072
D	LEU59
D	THR120
D	GLY121
D	SER122
D	TYR148
D	HIS149
D	GLY150
D	GLU237
D	VAL242
D	ASP269
D	VAL271
D	LEU272
D	LYS298
D	ARG442
D	HOH2043

---

site_id	AC5
Number of Residues	16
Details	BINDING SITE FOR RESIDUE PDA E 1000

Chain	Residue
E	LEU59
E	GLY121
E	SER122
E	TYR148
E	HIS149
E	GLU237
E	VAL242
E	ASP269
E	VAL271
E	LEU272
E	LYS298
E	ARG442
E	HOH2025
E	HOH2027
F	VAL328
F	THR330

---

site_id	AC6
Number of Residues	16
Details	BINDING SITE FOR RESIDUE PDA F 1000

Chain	Residue
F	TYR148
F	HIS149
F	GLU237
F	ASP269
F	VAL271
F	LEU272
F	LYS298
F	ARG442
E	VAL328
E	THR330
E	HOH2052
E	HOH2053
F	LEU59
F	THR120
F	GLY121
F	SER122

---

site_id	AC7
Number of Residues	20
Details	BINDING SITE FOR RESIDUE PDA G 1000

Chain	Residue
G	LEU59
G	GLY121
G	SER122
G	TYR148
G	HIS149
G	GLY150
G	GLU237
G	VAL242
G	ASP269
G	VAL271
G	LEU272
G	LYS298
G	ARG442
G	HOH2040
G	HOH2041
G	HOH2052
G	HOH2089
G	HOH2090
H	VAL328
H	THR330

---

site_id	AC8
Number of Residues	17
Details	BINDING SITE FOR RESIDUE PDA H 1000

Chain	Residue
G	VAL328
G	THR330
G	HOH2042
G	HOH2075
G	HOH2076
G	HOH2077
H	LEU59
H	GLY121
H	SER122
H	TYR148
H	HIS149
H	VAL242
H	ASP269
H	VAL271
H	LYS298
H	ARG442
H	HOH2032

---

site_id	AC9
Number of Residues	18
Details	BINDING SITE FOR RESIDUE PDA I 1000

Chain	Residue
I	LEU59
I	THR120
I	GLY121
I	SER122
I	TYR148
I	HIS149
I	GLU237
I	VAL242
I	ASP269
I	VAL271
I	LEU272
I	LYS298
I	ARG442
I	HOH2015
I	HOH2018
J	VAL328
J	SER329
J	THR330

---

site_id	BC1
Number of Residues	14
Details	BINDING SITE FOR RESIDUE PDA J 1000

Chain	Residue
I	VAL328
I	SER329
I	THR330
J	GLY121
J	SER122
J	TYR148
J	HIS149
J	GLU237
J	VAL242
J	ASP269
J	VAL271
J	LEU272
J	LYS298
J	ARG442

---

site_id	BC2
Number of Residues	14
Details	BINDING SITE FOR RESIDUE PDA K 1000

Chain	Residue
K	THR120
K	GLY121
K	SER122
K	TYR148
K	HIS149
K	GLU237
K	VAL242
K	ASP269
K	VAL271
K	LEU272
K	LYS298
K	ARG442
L	VAL328
L	THR330

---

site_id	BC3
Number of Residues	15
Details	BINDING SITE FOR RESIDUE PDA L 1000

Chain	Residue
K	SER329
K	THR330
L	LEU59
L	THR120
L	GLY121
L	SER122
L	TYR148
L	HIS149
L	GLU237
L	VAL242
L	ASP269
L	VAL271
L	LEU272
L	LYS298
L	ARG442

---

Functional Information from PROSITE/UniProt

site_id	PS00599
Number of Residues	10
Details	AA_TRANSFER_CLASS_2 Aminotransferases class-II pyridoxal-phosphate attachment site. TMGKGLSSSS

Chain	Residue	Details
A	THR295-SER304

---

site_id	PS00600
Number of Residues	38
Details	AA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. WIsDEVlt.GFgRtGkwfgyqhygvqp....DIItmGKglsSS

Chain	Residue	Details
A	TRP266-SER303

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