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	L-arginine biosynthetic process
A	0008483	molecular_function	transaminase activity
A	0008652	biological_process	amino acid biosynthetic process
A	0016740	molecular_function	transferase 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	L-arginine biosynthetic process
B	0008483	molecular_function	transaminase activity
B	0008652	biological_process	amino acid biosynthetic process
B	0016740	molecular_function	transferase 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	L-arginine biosynthetic process
C	0008483	molecular_function	transaminase activity
C	0008652	biological_process	amino acid biosynthetic process
C	0016740	molecular_function	transferase 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	L-arginine biosynthetic process
D	0008483	molecular_function	transaminase activity
D	0008652	biological_process	amino acid biosynthetic process
D	0016740	molecular_function	transferase 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	32
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01107","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	4
Details	Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"HAMAP-Rule","id":"MF_01107","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	8
Details	Cross-link: {"description":"Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)","evidences":[{"source":"PubMed","id":"20066036","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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