4E3R

PLP-bound aminotransferase mutant crystal structure from Vibrio fluvialis

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003867	molecular_function	4-aminobutyrate transaminase activity
A	0004015	molecular_function	adenosylmethionine-8-amino-7-oxononanoate transaminase activity
A	0008483	molecular_function	transaminase activity
A	0009102	biological_process	biotin biosynthetic process
A	0009448	biological_process	gamma-aminobutyric acid metabolic process
A	0016740	molecular_function	transferase activity
A	0030170	molecular_function	pyridoxal phosphate binding
B	0003867	molecular_function	4-aminobutyrate transaminase activity
B	0004015	molecular_function	adenosylmethionine-8-amino-7-oxononanoate transaminase activity
B	0008483	molecular_function	transaminase activity
B	0009102	biological_process	biotin biosynthetic process
B	0009448	biological_process	gamma-aminobutyric acid metabolic process
B	0016740	molecular_function	transferase activity
B	0030170	molecular_function	pyridoxal phosphate binding
C	0003867	molecular_function	4-aminobutyrate transaminase activity
C	0004015	molecular_function	adenosylmethionine-8-amino-7-oxononanoate transaminase activity
C	0008483	molecular_function	transaminase activity
C	0009102	biological_process	biotin biosynthetic process
C	0009448	biological_process	gamma-aminobutyric acid metabolic process
C	0016740	molecular_function	transferase activity
C	0030170	molecular_function	pyridoxal phosphate binding
D	0003867	molecular_function	4-aminobutyrate transaminase activity
D	0004015	molecular_function	adenosylmethionine-8-amino-7-oxononanoate transaminase activity
D	0008483	molecular_function	transaminase activity
D	0009102	biological_process	biotin biosynthetic process
D	0009448	biological_process	gamma-aminobutyric acid metabolic process
D	0016740	molecular_function	transferase activity
D	0030170	molecular_function	pyridoxal phosphate binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	10
Details	BINDING SITE FOR RESIDUE SO4 A 501

Chain	Residue
A	PRO4
B	HOH719
A	GLN5
A	SER6
A	ALA9
B	GLN5
B	SER6
B	ALA9
B	SO4501
B	HOH663

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site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NA A 502

Chain	Residue
A	VAL101
A	GLU102
A	SER104
A	PHE106
A	HOH718
A	HOH735

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site_id	AC3
Number of Residues	12
Details	BINDING SITE FOR RESIDUE SO4 B 501

Chain	Residue
A	ALA9
A	SO4501
A	HOH846
B	PRO4
B	GLN5
B	ALA9
B	THR13
B	HOH663
B	HOH803
B	HOH897
B	HOH922
B	HOH941

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site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NA B 502

Chain	Residue
B	VAL101
B	GLU102
B	SER104
B	PHE106
B	HOH689
B	HOH697

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site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NA C 501

Chain	Residue
C	VAL101
C	GLU102
C	SER104
C	PHE106
C	HOH801

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site_id	AC6
Number of Residues	11
Details	BINDING SITE FOR RESIDUE SO4 D 501

Chain	Residue
C	PRO4
C	GLN5
C	SER6
C	ALA9
C	HOH601
C	HOH909
D	GLN5
D	SER6
D	ALA9
D	HOH690
D	HOH849

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site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NA D 502

Chain	Residue
D	VAL101
D	GLU102
D	SER104
D	PHE106
D	HOH652
D	HOH669

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Functional Information from PROSITE/UniProt

site_id	PS00600
Number of Residues	38
Details	AA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. VIsDEVvc.GFgRtGntwgcvtydftp....DAIisSKnltAG

Chain	Residue	Details
A	VAL253-GLY290

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