Structure of PDB 8ht4 Chain B

Receptor sequence
>8ht4B (length=390) Species: 196627 (Corynebacterium glutamicum ATCC 13032) [Search protein sequence]
STLETWPQVIINTYGTPPVELVSGKGATVTDDQGNVYIDLLAGIAVNALG
HAHPAIIEAVTNQIGQLGHVSNLFASRPVVEVAEELIKRFSLDDATLAAQ
TRVFFCNSGAEANEAAFKIARLTGRSRILAAVHGFHGRTMGSLALTGQPD
KREAFLPMPSGVEFYPYGDTDYLRKMVETNPTDVAAIFLEPIQGETGVVP
APEGFLKAVRELCDEYGILMITDEVQTGVGRTGDFFAHQHDGVVPDVVTM
AKGLGGGLPIGACLATGRAAELMTPGKHGTTFGGNPVACAAAKAVLSVVD
DAFCAEVARKGELFKELLAKVDGVVDVRGRGLMLGVVLERDVAKQAVLDG
FKHGVILNAPADNIIRLTPPLVITDEEIADAVKAIAETIA
3D structure
PDB8ht4 Structural and functional characterization of acetylornithine aminotransferase from corynebacterium glutamicum
ChainB
Resolution2.51 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
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 S109 G110 A111 F136 H137 E191 D224 V226 Q227 K253 S108 G109 A110 F135 H136 E190 D223 V225 Q226 K252
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:8ht4, PDBe:8ht4, PDBj:8ht4
PDBsum8ht4
PubMed37230944
UniProtQ59282|ARGD_CORGL Acetylornithine aminotransferase (Gene Name=argD)

[Back to BioLiP]