Structure of PDB 6aph Chain A

Receptor sequence

>6aphA (length=432) Species: 1338011 (Elizabethkingia anophelis NUHP1) [Search protein sequence]

QYVPYKVKDISLAEWGRKEIELAEAEMPGLMAIREEYGPQQPLKGARIAG
CLHMTIQTAVLIETLVALGADVTWSSCNIFSTQDHAAAAIAAAGIPVYAW
KGMNEEEFDWCIEQTLFFGEDRQPLNMILDDGGDLTNMVFDKYPELTKDI
KGLSEETTTGVHRLYERMQNGTLVMPAINVNDSVTKSKFDNKYGCRESAV
DAIRRATDVMLAGKRVVVCGFGDVGKGTAASFRGAGSIVTVTEIDPICAL
QAAMEGYEVKQLDTVVDNADIIITTTGNFGIVRGEHFEKMKDKTIVCNIG
HFDNEIDMAWLNKNHGATKVEIKPQVDKYNVNGNDIIILAEGRLVNLGCA
TGHPSFVMSNSFSNQTLAQIELWVHSDKYENKVYTLPKHLDEKVAALHLK
KLGVELETLSEEQAKYIGVTVDGPFKPDYYRY

3D structure

PDB

6aph Crystal structure of Adenosylhomocysteinase from Elizabethkingia anophelis NUHP1 in complex with NAD and Adenosine

Chain

Resolution

1.65 Å

3D
structure

Catalytic site residues are labeled in the structure
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Enzymatic activity

Catalytic site (original residue number in PDB)	H58 S81 S86 D136 E161 N186 K191 D195 N196 C200 H306 H358 S366 Q370
Catalytic site (residue number reindexed from 1)	H53 S76 S81 D131 E156 N181 K186 D190 N191 C195 H301 H353 S361 Q365
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	A	T162 T163 T164 N196 G227 D228 V229 E248 I249 T281 N283 I286 I304 G305 H306 N351 H358	T157 T158 T159 N191 G222 D223 V224 E243 I244 T276 N278 I281 I299 G300 H301 N346 H353
BS02	ADN	A	L57 H58 T60 Q62 D136 T162 D195 H306 G357 H358 M363	L52 H53 T55 Q57 D131 T157 D190 H301 G352 H353 M358

Gene Ontology

	Molecular Function
GO:0000166	nucleotide binding
GO:0004013	adenosylhomocysteinase activity
GO:0016787	hydrolase activity

	Biological Process
GO:0006730	one-carbon metabolic process
GO:0033353	S-adenosylmethionine cycle
GO:0071269	L-homocysteine biosynthetic process

	Cellular Component
GO:0005737	cytoplasm
GO:0005829	cytosol

View graph for
Molecular Function

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Biological Process

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Cellular Component

External links

PDB	RCSB:6aph, PDBe:6aph, PDBj:6aph
PDBsum	6aph
PubMed
UniProt	A0A077EDS4

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