Structure of PDB 2ord Chain B

Receptor sequence

>2ordB (length=393) Species: 243274 (Thermotoga maritima MSB8)

KIHHHHHHMYLMNTYSRFPATFVYGKGSWIYDEKGNAYLDFTSGIAVNVL
GHSHPRLVEAIKDQAEKLIHCSNLFWNRPQMELAELLSKNTFGGKVFFAN
TGTEANEAAIKIARKYGKKKSEKKYRILSAHNSFHGRTLGSLTATGQPKY
QKPFEPLVPGFEYFEFNNVEDLRRKMSEDVCAVFLEPIQGESGIVPATKE
FLEEARKLCDEYDALLVFDEVQCGMGRTGKLFAYQKYGVVPDVLTTAKGL
GGGVPIGAVIVNERANVLEPGDHGTTFGGNPLACRAGVTVIKELTKEGFL
EEVEEKGNYLMKKLQEMKEEYDVVADVRGMGLMIGIQFREEVSNREVATK
CFENKLLVVPAGNNTIRFLPPLTVEYGEIDLAVETLKKVLQGI

3D structure

• PDB: 2ord Crystal structure of Acetylornithine aminotransferase (EC 2.6.1.11) (ACOAT) (TM1785) from Thermotoga maritima at 1.40 A resolution
• Chain: B
• Resolution: 1.4 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): F126 E178 D211 Q214 K240 T268 R359
• Catalytic site (residue number reindexed from 1): F134 E186 D219 Q222 K248 T276 R367
• 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	PLP	B	G94 T95 F126 H127 E178 D211 V213 Q214 K240	G102 T103 F134 H135 E186 D219 V221 Q222 K248

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:2ord, PDBe:2ord, PDBj:2ord
• PDBsum: 2ord
• UniProt: Q9X2A5|ARGD_THEMA Acetylornithine aminotransferase (Gene Name=argD)