Structure of PDB 2jg7 Chain G

Receptor sequence
>2jg7G (length=509) Species: 72011 (Acanthopagrus schlegelii) [Search protein sequence]
SGLLINQPKYSWLKELGLSEDNPGVYNGSWGGSGEVITSYCPANNEPIAR
VTQATLAEYEETVQKTREAWKMWADIPAPKRGEIVRQIGDALRKKIKVLG
SLVSLEMGKIYVEGVGEVQEYVDVCDYAVGLSRMIGGPVLPSERPGHALI
EQWNPVGLVGIITAFNFPVAVYGWNNAIALTCGNVCLWKGAPTTPLTSVA
VTKIVAEVLEQNNLPGAICSMTCGGADIGTAMAKDERVDLLSFTGSTHVG
KMVAMMVQERFGRKLLELGGNNAIIVFEDADLNLVVPSAVFASVGTAGQR
CTTTRRLMLHESVHDAVVERIAKAYKQVRIGDPWDPSTLYGPLHTKQAVD
QYLAAIEQAKQQGGTLVCGGKVMDRPGNYVEPTIITGLAHDAPIVHTETF
VPILYVLKFKTEEEAFAWNNEVQQGLSSSIFTKDLGRVFRWLGPKGSDCG
IVNVNIPTSGAEIGGAFGGEKHTGGGRESGSDSWKQYMRRSTCTINYSKD
LPLAQGIKF
3D structure
PDB2jg7 The Crystal Structure of Seabream Antiquitin Reveals the Structural Basis of its Substrate Specificity.
ChainG
Resolution2.83 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) N166 K189 E267 C301 E398 E478
Catalytic site (residue number reindexed from 1) N166 K189 E267 C301 E398 E478
Enzyme Commision number 1.2.1.3: aldehyde dehydrogenase (NAD(+)).
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 NAD G I162 T163 A164 F165 N166 K189 P192 A226 G229 T230 F243 T244 G245 S246 V249 E267 L268 C301 E398 F400 I162 T163 A164 F165 N166 K189 P192 A226 G229 T230 F243 T244 G245 S246 V249 E267 L268 C301 E398 F400
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004029 aldehyde dehydrogenase (NAD+) activity
GO:0016491 oxidoreductase activity
GO:0016620 oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor

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Molecular Function
External links
PDB RCSB:2jg7, PDBe:2jg7, PDBj:2jg7
PDBsum2jg7
PubMed18694748
UniProtQ4KTQ7

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