Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6U7A

Rv3722c in complex with kynurenine

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004069	molecular_function	L-aspartate:2-oxoglutarate aminotransferase activity
A	0005576	cellular_component	extracellular region
A	0008483	molecular_function	transaminase activity
A	0016740	molecular_function	transferase activity
B	0004069	molecular_function	L-aspartate:2-oxoglutarate aminotransferase activity
B	0005576	cellular_component	extracellular region
B	0008483	molecular_function	transaminase activity
B	0016740	molecular_function	transferase activity
C	0004069	molecular_function	L-aspartate:2-oxoglutarate aminotransferase activity
C	0005576	cellular_component	extracellular region
C	0008483	molecular_function	transaminase activity
C	0016740	molecular_function	transferase activity
D	0004069	molecular_function	L-aspartate:2-oxoglutarate aminotransferase activity
D	0005576	cellular_component	extracellular region
D	0008483	molecular_function	transaminase activity
D	0016740	molecular_function	transferase activity
E	0004069	molecular_function	L-aspartate:2-oxoglutarate aminotransferase activity
E	0005576	cellular_component	extracellular region
E	0008483	molecular_function	transaminase activity
E	0016740	molecular_function	transferase activity
F	0004069	molecular_function	L-aspartate:2-oxoglutarate aminotransferase activity
F	0005576	cellular_component	extracellular region
F	0008483	molecular_function	transaminase activity
F	0016740	molecular_function	transferase activity
G	0004069	molecular_function	L-aspartate:2-oxoglutarate aminotransferase activity
G	0005576	cellular_component	extracellular region
G	0008483	molecular_function	transaminase activity
G	0016740	molecular_function	transferase activity
H	0004069	molecular_function	L-aspartate:2-oxoglutarate aminotransferase activity
H	0005576	cellular_component	extracellular region
H	0008483	molecular_function	transaminase activity
H	0016740	molecular_function	transferase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	23
Details	binding site for residue Q0P A 501

Chain	Residue
A	ARG36
A	ASN189
A	ASP218
A	ALA220
A	TYR221
A	SER254
A	SER256
A	LYS257
A	PHE349
A	ARG392
A	HOH619
A	GLY37
A	HOH625
A	HOH673
A	HOH677
B	TYR69
A	LYS38
A	SER99
A	SER100
A	LEU101
A	TYR139
A	ARG141
A	VAL184

site_id	AC2
Number of Residues	4
Details	binding site for residue PO4 A 502

Chain	Residue
A	ARG59
A	ASP65
A	HOH622
H	ASP56

site_id	AC3
Number of Residues	4
Details	binding site for residue GOL A 503

Chain	Residue
A	ASP305
D	PHE300
D	GLY306
D	HOH637

site_id	AC4
Number of Residues	5
Details	binding site for residue GOL A 504

Chain	Residue
A	GLU169
A	ARG201
A	ARG202
A	GLN205
F	ARG360

site_id	AC5
Number of Residues	5
Details	binding site for residue 1PE A 505

Chain	Residue
A	PHE300
A	PHE301
A	GLY306
A	HOH638
D	ASP305

site_id	AC6
Number of Residues	6
Details	binding site for residue KYA B 501

Chain	Residue
A	TYR69
B	GLY37
B	TYR139
B	ARG141
B	LYS257
B	PMP502

site_id	AC7
Number of Residues	17
Details	binding site for residue PMP B 502

Chain	Residue
A	TYR69
B	SER99
B	SER100
B	LEU101
B	TYR139
B	VAL184
B	ASN189
B	ASP218
B	ALA220
B	TYR221
B	SER254
B	SER256
B	LYS257
B	KYA501
B	HOH610
B	HOH619
B	HOH702

site_id	AC8
Number of Residues	8
Details	binding site for residue GOL B 503

Chain	Residue
B	GLY71
B	GLN72
B	HIS73
B	GLY74
B	HOH611
B	HOH620
B	HOH649
B	HOH656

site_id	AC9
Number of Residues	6
Details	binding site for residue GOL B 504

Chain	Residue
B	GLY87
B	ILE88
B	ALA89
B	ASN92
B	ASP235
B	HOH607

site_id	AD1
Number of Residues	7
Details	binding site for residue 1PE B 505

Chain	Residue
B	GLU42
B	LEU46
B	ARG313
B	ILE317
C	GLU42
C	ASP45
C	LEU46

site_id	AD2
Number of Residues	9
Details	binding site for residue KYA C 501

Chain	Residue
C	GLY37
C	LYS38
C	TYR139
C	ARG141
C	ASN189
C	LYS257
C	PHE349
C	PMP502
H	TYR69

site_id	AD3
Number of Residues	17
Details	binding site for residue PMP C 502

Chain	Residue
C	ASN189
C	ASP218
C	ALA220
C	TYR221
C	SER254
C	SER256
C	LYS257
C	KYA501
C	HOH614
C	HOH631
C	HOH675
H	TYR69
C	SER99
C	SER100
C	LEU101
C	TYR139
C	VAL184

site_id	AD4
Number of Residues	6
Details	binding site for residue PO4 C 503

Chain	Residue
C	ASP161
C	SER196
C	GLU198
C	HOH693
F	LYS131
F	GLU152

site_id	AD5
Number of Residues	2
Details	binding site for residue GOL C 504

Chain	Residue
C	TYR382
C	LYS384

site_id	AD6
Number of Residues	9
Details	binding site for residue KYA D 501

Chain	Residue
D	GLY37
D	LYS38
D	TYR139
D	ARG141
D	LYS257
D	PHE349
D	PMP502
D	GOL504
E	TYR69

site_id	AD7
Number of Residues	17
Details	binding site for residue PMP D 502

Chain	Residue
D	SER99
D	SER100
D	LEU101
D	TYR139
D	VAL184
D	ASN189
D	ASP218
D	ALA220
D	TYR221
D	SER254
D	SER256
D	LYS257
D	KYA501
D	HOH625
D	HOH656
D	HOH702
E	TYR69

site_id	AD8
Number of Residues	4
Details	binding site for residue PO4 D 503

Chain	Residue
C	ARG360
C	ARG361
D	ARG201
D	ARG202

site_id	AD9
Number of Residues	5
Details	binding site for residue GOL D 504

Chain	Residue
D	THR35
D	GLY37
D	ASP140
D	ARG392
D	KYA501

site_id	AE1
Number of Residues	2
Details	binding site for residue 1PE D 505

Chain	Residue
D	TYR382
D	LYS384

site_id	AE2
Number of Residues	16
Details	binding site for residue PLP E 501

Chain	Residue
D	TYR69
E	SER99
E	SER100
E	LEU101
E	TYR139
E	VAL184
E	ASN189
E	ASP218
E	ALA220
E	TYR221
E	SER254
E	SER256
E	LYS257
E	HOH607
E	HOH679
E	HOH680

site_id	AE3
Number of Residues	4
Details	binding site for residue 1PE E 502

Chain	Residue
E	GLU42
E	1PE503
F	GLU42
F	LEU46

site_id	AE4
Number of Residues	6
Details	binding site for residue 1PE E 503

Chain	Residue
E	GLN49
E	PHE300
E	GLY306
E	ARG313
E	1PE502
F	GLU42

site_id	AE5
Number of Residues	16
Details	binding site for residue PLP F 501

Chain	Residue
F	SER99
F	SER100
F	LEU101
F	TYR139
F	VAL184
F	ASN189
F	ASP218
F	ALA220
F	TYR221
F	SER254
F	SER256
F	LYS257
F	HOH612
F	HOH658
F	HOH693
G	TYR69

site_id	AE6
Number of Residues	7
Details	binding site for residue KYA G 501

Chain	Residue
F	TYR69
F	ILE287
G	GLY37
G	TYR139
G	ARG141
G	PHE349
G	PMP502

site_id	AE7
Number of Residues	17
Details	binding site for residue PMP G 502

Chain	Residue
F	TYR69
G	SER99
G	SER100
G	LEU101
G	TYR139
G	VAL184
G	ASN189
G	ASP218
G	ALA220
G	TYR221
G	SER254
G	SER256
G	LYS257
G	KYA501
G	HOH638
G	HOH662
G	HOH698

site_id	AE8
Number of Residues	5
Details	binding site for residue PO4 G 503

Chain	Residue
D	ASP56
F	PHE397
G	ARG59
G	ASP65
G	HOH664

site_id	AE9
Number of Residues	4
Details	binding site for residue PO4 G 504

Chain	Residue
G	GLU169
G	MET206
G	ARG207
G	GOL508

site_id	AF1
Number of Residues	5
Details	binding site for residue GOL G 505

Chain	Residue
D	ASP57
D	ASP60
D	PRO61
G	ASP57
G	ARG59

site_id	AF2
Number of Residues	4
Details	binding site for residue GOL G 506

Chain	Residue
G	PHE300
G	GLY306
G	HOH670
H	ASP305

site_id	AF3
Number of Residues	6
Details	binding site for residue GOL G 507

Chain	Residue
G	GLY87
G	ALA89
G	ASN92
G	ASP235
G	LEU237
G	HOH663

site_id	AF4
Number of Residues	5
Details	binding site for residue GOL G 508

Chain	Residue
B	ARG360
G	GLU169
G	ARG201
G	ARG202
G	PO4504

site_id	AF5
Number of Residues	16
Details	binding site for residue PLP H 501

Chain	Residue
C	TYR69
H	SER99
H	SER100
H	LEU101
H	TYR139
H	VAL184
H	ASN189
H	ASP218
H	ALA220
H	TYR221
H	SER254
H	SER256
H	LYS257
H	HOH617
H	HOH632
H	HOH656

site_id	AF6
Number of Residues	5
Details	binding site for residue PO4 H 502

Chain	Residue
E	ARG360
E	ARG361
H	GLU198
H	ARG201
H	ARG202

site_id	AF7
Number of Residues	2
Details	binding site for residue 1PE H 503

Chain	Residue
H	TYR382
H	LYS384

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	48
Details	Binding site: {"evidences":[{"source":"PubMed","id":"32327655","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUN-2015","submissionDatabase":"PDB data bank","title":"Rv3722c aminotransferase from Mycobacterium tuberculosis.","authoringGroup":["Structures of Mtb proteins conferring susceptibility to known Mtb inhibitors (MTBI)"],"authors":["Osipiuk J.","Hatzos-Skintges C.","Jedrzejczak R.","Babnigg G.","Sacchettini J.","Joachimiak A."]}}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	24
Details	Binding site: {"evidences":[{"source":"PubMed","id":"32327655","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)