Structure of PDB 1k0u Chain F

Receptor sequence

>1k0uF (length=430) Species: 10116 (Rattus norvegicus) [Search protein sequence]

DKLPYKVADIGLAAWGRKALDIAENEMPGLMRMREMYSASKPLKGARIAG
CLHMTVETAVLIETLVALGAEVRWSSCNIFSTQDHAAAAIAKAGIPVFAW
KGETDEEYLWCIEQTLHFKDGPLNMILDDGGDLTNLIHTKHPQLLSGIRG
ISEETTTGVHNLYKMMANGILKVPAINVNDSVTKSKFDNLYGCRESLIDG
IKRATDVMIAGKVAVVAGYGDVGKGCAQALRGFGARVIITEIDPINALQA
AMEGYEVTTMDEACKEGNIFVTTTGCVDIILGRHFEQMKDDAIVCNIGHF
DVEIDVKWLNENAVEKVNIKPQVDRYLLKNGHRIILLAEGRLVNLGCAMG
HPSFVMSNSFTNQVMAQIELWTHPDKYPVGVHFLPKKLDEAVAEAHLGKL
NVKLTKLTEKQAQYLGMPINGPFKPDHYRY

3D structure

PDB

1k0u Inhibition of S-adenosylhomocysteine hydrolase by acyclic sugar adenosine analogue D-eritadenine. Crystal structure of S-adenosylhomocysteine hydrolase complexed with D-eritadenine.

Chain

Resolution

3.0 Å

3D
structure

Catalytic site residues are labeled in the structure
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Enzymatic activity

Catalytic site (original residue number in PDB)	H54 S77 S82 D130 E155 N180 K185 D189 N190 C194 H300 H352 S360 Q364
Catalytic site (residue number reindexed from 1)	H53 S76 S81 D129 E154 N179 K184 D188 N189 C193 H299 H351 S359 Q363
Enzyme Commision number	3.13.2.1: adenosylhomocysteinase.

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	F	K425 Y429	K424 Y428
BS02	NAD	F	T156 T157 T158 N190 G219 G221 V223 T241 E242 I243 N247 T274 T275 I280 I298 G299 H300 L343 N345 H352	T155 T156 T157 N189 G218 G220 V222 T240 E241 I242 N246 T273 T274 I279 I297 G298 H299 L342 N344 H351
BS03	DEA	F	T56 E58 D130 E155 T156 K185 D189 L346 G351 H352 M357	T55 E57 D129 E154 T155 K184 D188 L345 G350 H351 M356	BindingDB: IC50=30nM

Gene Ontology

	Molecular Function
GO:0004013	adenosylhomocysteinase activity
GO:0005507	copper ion binding
GO:0016787	hydrolase activity
GO:0030554	adenyl nucleotide binding
GO:0042802	identical protein binding
GO:0051287	NAD binding
GO:0098604	adenosylselenohomocysteinase activity

	Biological Process
GO:0001666	response to hypoxia
GO:0002439	chronic inflammatory response to antigenic stimulus
GO:0006730	one-carbon metabolic process
GO:0007584	response to nutrient
GO:0019510	S-adenosylhomocysteine catabolic process
GO:0033353	S-adenosylmethionine cycle
GO:0042745	circadian sleep/wake cycle

	Cellular Component
GO:0005634	nucleus
GO:0005737	cytoplasm
GO:0005783	endoplasmic reticulum
GO:0005829	cytosol
GO:0042470	melanosome

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Molecular Function

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Biological Process

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Cellular Component

External links

PDB	RCSB:1k0u, PDBe:1k0u, PDBj:1k0u
PDBsum	1k0u
PubMed	11741948
UniProt	P10760\|SAHH_RAT Adenosylhomocysteinase (Gene Name=Ahcy)

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