Structure of PDB 1wkh Chain A

Receptor sequence
>1wkhA (length=387) Species: 274 (Thermus thermophilus) [Search protein sequence]
WRALLEAEKTLDSGVYNKHDLLIVRGQGARVWDAEGNEYIDCVGGYGVAN
LGHGNPEVVEAVKRQAETLMAMPQTLPTPMRGEFYRTLTAILPPELNRVF
PVNSGTEANEAALKFARAHTGRKKFVAAMRGFSGRTMGSLSVTWEPKYRE
PFLPLVEPVEFIPYNDVEALKRAVDEETAAVILEPVQGEGGVRPATPEFL
RAAREITQEKGALLILDEIQTGMGRTGKRFAFEHFGIVPDILTLAKALGG
GVPLGVAVMREEVARSMPKGGHGTTFGGNPLAMAAGVAAIRYLERTRLWE
RAAELGPWFMEKLRAIPSPKIREVRGMGLMVGLELKEKAAPYIARLEKEH
RVLALQAGPTVIRFLPPLVIEKEDLERVVEAVRAVLA
3D structure
PDB1wkh Acetylornithine aminotransferase from thermus thermophilus HB8
ChainA
Resolution2.25 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S21 F140 E192 D225 Q228 K254 T283 R371
Catalytic site (residue number reindexed from 1) S13 F132 E184 D217 Q220 K246 T275 R363
Enzyme Commision number 2.6.1.118: [amino group carrier protein]-gamma-(L-lysyl)-L-glutamate aminotransferase.
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 PPE A Y54 S112 G113 T114 F140 S141 E192 E197 D225 I227 K254 R371 Y46 S104 G105 T106 F132 S133 E184 E189 D217 I219 K246 R363
Gene Ontology
Molecular Function
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
GO:0009085 lysine biosynthetic process
GO:0019878 lysine biosynthetic process via aminoadipic acid
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:1wkh, PDBe:1wkh, PDBj:1wkh
PDBsum1wkh
PubMed
UniProtQ5SHH5|LYSJ_THET8 [LysW]-aminoadipate semialdehyde transaminase (Gene Name=lysJ)

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