6Q1R

A hypothetical aminotransferase from Mycobacterium tuberculosis, PLP-bound form

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0008360	biological_process	regulation of cell shape
A	0008483	molecular_function	transaminase activity
A	0008696	molecular_function	4-amino-4-deoxychorismate lyase activity
A	0009252	biological_process	peptidoglycan biosynthetic process
A	0016829	molecular_function	lyase activity
A	0019752	biological_process	carboxylic acid metabolic process
A	0030170	molecular_function	pyridoxal phosphate binding
A	0046394	biological_process	carboxylic acid biosynthetic process
A	0046654	biological_process	tetrahydrofolate biosynthetic process
A	0046656	biological_process	folic acid biosynthetic process
B	0003824	molecular_function	catalytic activity
B	0005829	cellular_component	cytosol
B	0005886	cellular_component	plasma membrane
B	0008360	biological_process	regulation of cell shape
B	0008483	molecular_function	transaminase activity
B	0008696	molecular_function	4-amino-4-deoxychorismate lyase activity
B	0009252	biological_process	peptidoglycan biosynthetic process
B	0016829	molecular_function	lyase activity
B	0019752	biological_process	carboxylic acid metabolic process
B	0030170	molecular_function	pyridoxal phosphate binding
B	0046394	biological_process	carboxylic acid biosynthetic process
B	0046654	biological_process	tetrahydrofolate biosynthetic process
B	0046656	biological_process	folic acid biosynthetic process
C	0003824	molecular_function	catalytic activity
C	0005829	cellular_component	cytosol
C	0005886	cellular_component	plasma membrane
C	0008360	biological_process	regulation of cell shape
C	0008483	molecular_function	transaminase activity
C	0008696	molecular_function	4-amino-4-deoxychorismate lyase activity
C	0009252	biological_process	peptidoglycan biosynthetic process
C	0016829	molecular_function	lyase activity
C	0019752	biological_process	carboxylic acid metabolic process
C	0030170	molecular_function	pyridoxal phosphate binding
C	0046394	biological_process	carboxylic acid biosynthetic process
C	0046654	biological_process	tetrahydrofolate biosynthetic process
C	0046656	biological_process	folic acid biosynthetic process
D	0003824	molecular_function	catalytic activity
D	0005829	cellular_component	cytosol
D	0005886	cellular_component	plasma membrane
D	0008360	biological_process	regulation of cell shape
D	0008483	molecular_function	transaminase activity
D	0008696	molecular_function	4-amino-4-deoxychorismate lyase activity
D	0009252	biological_process	peptidoglycan biosynthetic process
D	0016829	molecular_function	lyase activity
D	0019752	biological_process	carboxylic acid metabolic process
D	0030170	molecular_function	pyridoxal phosphate binding
D	0046394	biological_process	carboxylic acid biosynthetic process
D	0046654	biological_process	tetrahydrofolate biosynthetic process
D	0046656	biological_process	folic acid biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	15
Details	binding site for residue PLP A 301

Chain	Residue
A	HIS47
A	LEU213
A	GLY215
A	THR216
A	THR217
A	SER253
A	HOH420
A	ARG50
A	LYS149
A	TYR153
A	GLU182
A	GLY183
A	PRO184
A	SER186
A	THR187

---

site_id	AC2
Number of Residues	4
Details	binding site for residue CIT A 302

Chain	Residue
A	LEU65
A	ARG69
A	ARG238
C	ARG121

---

site_id	AC3
Number of Residues	5
Details	binding site for residue GOL A 303

Chain	Residue
A	TYR179
A	TYR210
A	HOH417
C	HIS261
C	ARG267

---

site_id	AC4
Number of Residues	5
Details	binding site for residue CIT C 302

Chain	Residue
A	ARG121
C	LEU65
C	PRO66
C	ARG69
C	ARG238

---

site_id	AC5
Number of Residues	16
Details	binding site for Di-peptide PLP B 301 and LYS B 149

Chain	Residue
B	VAL30
B	PHE31
B	ARG50
B	SER54
B	ALA148
B	THR150
B	TYR153
B	GLU182
B	GLY183
B	PRO184
B	SER186
B	LEU213
B	THR216
B	THR217
B	SER252
B	SER253

---

site_id	AC6
Number of Residues	18
Details	binding site for Di-peptide PLP C 301 and LYS C 149

Chain	Residue
C	VAL30
C	PHE31
C	HIS47
C	ARG50
C	SER54
C	ALA148
C	THR150
C	TYR153
C	GLU182
C	GLY183
C	PRO184
C	SER186
C	THR187
C	LEU213
C	THR216
C	THR217
C	SER252
C	SER253

---

site_id	AC7
Number of Residues	19
Details	binding site for Di-peptide PLP D 301 and LYS D 149

Chain	Residue
D	VAL30
D	PHE31
D	ARG50
D	SER54
D	ALA148
D	THR150
D	TYR153
D	GLU182
D	GLY183
D	PRO184
D	ARG185
D	SER186
D	THR187
D	LEU213
D	GLY215
D	THR216
D	THR217
D	SER252
D	SER253

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	20
Details	BINDING: BINDING => ECO:0000269|PubMed:33950161, ECO:0007744|PDB:6Q1R, ECO:0007744|PDB:6Q1S

Chain	Residue	Details
A	ARG50
B	SER253
C	ARG50
C	TYR153
C	THR216
C	THR217
C	SER253
D	ARG50
D	TYR153
D	THR216
D	THR217
A	TYR153
D	SER253
A	THR216
A	THR217
A	SER253
B	ARG50
B	TYR153
B	THR216
B	THR217

---

site_id	SWS_FT_FI2
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269|PubMed:33950161, ECO:0007744|PDB:6Q1S

Chain	Residue	Details
A	SER252
D	SER252
D	MET254
D	THR255
A	MET254
A	THR255
B	SER252
B	MET254
B	THR255
C	SER252
C	MET254
C	THR255

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	SITE: Important for dual ACDL/DAAT activities => ECO:0000305|PubMed:33950161

Chain	Residue	Details
A	ARG26
B	ARG26
C	ARG26
D	ARG26

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:33950161, ECO:0007744|PDB:6Q1R

Chain	Residue	Details
A	LYS149
B	LYS149
C	LYS149
D	LYS149

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