Structure of PDB 2eh6 Chain A

Receptor sequence
>2eh6A (length=375) Species: 224324 (Aquifex aeolicus VF5) [Search protein sequence]
TYLMNNYARLPVKFVRGKGVYLYDEEGKEYLDFVSGIGVNSLGHAYPKLT
EALKEQVEKLLHVSNLYENPWQEELAHKLVKHFWTEGKVFFANSGTESVE
AAIKLARKYWRDKGKNKWKFISFENSFHGRTYGSLSATGQPKFHKGFEPL
VPGFSYAKLNDIDSVYKLLDEETAGIIIEVIQGEGGVNEASEDFLSKLQE
ICKEKDVLLIIDEVQTGIGRTGEFYAYQHFNLKPDVIALAKGLGGGVPIG
AILAREEVAQSFTPGSHGSTFGGNPLACRAGTVVVDEVEKLLPHVREVGN
YFKEKLKELGKGKVKGRGLMLGLELERECKDYVLKALEKGLLINCTAGKV
LRFLPPLIIQKEHIDRAISVLREIL
3D structure
PDB2eh6 Crystal structure of acetylornithine aminotransferase from Aquifex aeolicus VF5
ChainA
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) F127 E179 D212 Q215 K241 T270 R352
Catalytic site (residue number reindexed from 1) F127 E179 D212 Q215 K241 T270 R352
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 A G95 T96 F127 H128 E179 D212 V214 K241 G95 T96 F127 H128 E179 D212 V214 K241
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2eh6, PDBe:2eh6, PDBj:2eh6
PDBsum2eh6
PubMed
UniProtO66442|ARGD_AQUAE Acetylornithine aminotransferase (Gene Name=argD)

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