Structure of PDB 7nn4 Chain C

Receptor sequence

>7nn4C (length=391) Species: 83332 (Mycobacterium tuberculosis H37Rv)

TTATMRQRWQAVMMNNYGTPPIALASGDGAVVTDVDGRTYIDLLGGIAVN
VLGHRHPAVIEAVTRQMSTLGHTSNLYATEPGIALAEELVALLGADQRTR
VFFCNSGAEANEAAFKLSRLTGRTKLVAAHDAFHGRTMGSLALTGQPAKQ
TPFAPLPGDVTHVGYGDVDALAAAVDDHTAAVFLEPIMGESGVVVPPAGY
LAAARDITARRGALLVLDEVQTGMGRTGAFFAHQHDGITPDVVTLAKGLG
GGLPIGACLAVGPAAELLTPGLHGSTFGGNPVCAAAALAVLRVLASDGLV
RRAEVLGKSLRHGIEALGHPLIDHVRGRGLLLGIALTAPHAKDAEATARD
AGYLVNAAAPDVIRLAPPLIIAEAQLDGFVAALPAILDRAV

3D structure

• PDB: 7nn4 A fragment-based approach to assess the ligandability of ArgB, ArgC, ArgD and ArgF in the L-arginine biosynthetic pathway of Mycobacterium tuberculosis
• Chain: C
• Resolution: 1.47 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): F139 D224 K253
• Catalytic site (residue number reindexed from 1): F133 D218 K247
• Enzyme Commision number: 2.6.1.11: acetylornithine transaminase.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	BZJ	C	Y23 R142	Y17 R136
BS02	BZJ	C	V174 I213 R216 R217	V168 I207 R210 R211
BS03	BZJ	C	L82 G280	L76 G274

Gene Ontology

Molecular Function

• GO:0003992 N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity
• GO:0008483 transaminase activity
• GO:0030170 pyridoxal phosphate binding
• GO:0042802 identical protein binding

Biological Process

• GO:0006525 arginine metabolic process
• GO:0006526 L-arginine biosynthetic process

Cellular Component

• GO:0005737 cytoplasm

External links

• PDB: RCSB:7nn4, PDBe:7nn4, PDBj:7nn4
• PDBsum: 7nn4
• UniProt: P9WPZ7|ARGD_MYCTU Acetylornithine aminotransferase (Gene Name=argD)