7NNC

Crystal structure of Mycobacterium tuberculosis ArgD with prosthetic group pyridoxal-5'-phosphate and 6-Methoxyquinoline-3-carboxylic acid

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003992	molecular_function	N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity
A	0005737	cellular_component	cytoplasm
A	0006525	biological_process	arginine metabolic process
A	0006526	biological_process	arginine biosynthetic process
A	0008483	molecular_function	transaminase activity
A	0030170	molecular_function	pyridoxal phosphate binding
A	0042802	molecular_function	identical protein binding
B	0003992	molecular_function	N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity
B	0005737	cellular_component	cytoplasm
B	0006525	biological_process	arginine metabolic process
B	0006526	biological_process	arginine biosynthetic process
B	0008483	molecular_function	transaminase activity
B	0030170	molecular_function	pyridoxal phosphate binding
B	0042802	molecular_function	identical protein binding
C	0003992	molecular_function	N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity
C	0005737	cellular_component	cytoplasm
C	0006525	biological_process	arginine metabolic process
C	0006526	biological_process	arginine biosynthetic process
C	0008483	molecular_function	transaminase activity
C	0030170	molecular_function	pyridoxal phosphate binding
C	0042802	molecular_function	identical protein binding
D	0003992	molecular_function	N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity
D	0005737	cellular_component	cytoplasm
D	0006525	biological_process	arginine metabolic process
D	0006526	biological_process	arginine biosynthetic process
D	0008483	molecular_function	transaminase activity
D	0030170	molecular_function	pyridoxal phosphate binding
D	0042802	molecular_function	identical protein binding

Functional Information from PROSITE/UniProt

site_id	PS00600
Number of Residues	38
Details	AA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. LVlDEVqt.GMgRtGaffahqhdgitp....DVVtlAKglgGG

Chain	Residue	Details
A	LEU221-GLY258

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	24
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01107

Chain	Residue	Details
A	GLY113
B	ASP224
B	SER281
B	THR282
C	GLY113
C	PHE139
C	ARG142
C	ASP224
C	SER281
C	THR282
D	GLY113
A	PHE139
D	PHE139
D	ARG142
D	ASP224
D	SER281
D	THR282
A	ARG142
A	ASP224
A	SER281
A	THR282
B	GLY113
B	PHE139
B	ARG142

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site_id	SWS_FT_FI2
Number of Residues	4
Details	MOD_RES: N-acetylthreonine; partial => ECO:0000269|PubMed:17259624, ECO:0007744|PubMed:21969609

Chain	Residue	Details
A	THR2
B	THR2
C	THR2
D	THR2

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site_id	SWS_FT_FI3
Number of Residues	4
Details	MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000255|HAMAP-Rule:MF_01107

Chain	Residue	Details
A	LLP253
B	LLP253
C	LLP253
D	LLP253

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site_id	SWS_FT_FI4
Number of Residues	8
Details	CROSSLNK: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup) => ECO:0000269|PubMed:20066036

Chain	Residue	Details
A	LYS314
B	LYS314
C	LYS314
D	LYS314

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