Structure of PDB 4y1p Chain A

Receptor sequence
>4y1pA (length=335) Species: 330779 (Sulfolobus acidocaldarius DSM 639) [Search protein sequence]
GFVVALIQGDGIGPEVVSKSKTILARLNEKFSLPIEYIEVEAGDTTKNKF
GDALPKDSLRVIEKADMILKGPVGETAADVVVKLRLMYDLYANLRPAKSL
PGLNKFGDVDILVVRENTEDLYKGLEHVISDGVTVGIKVITRAASTRIAQ
VALNQALRRKKKVVCVHKSNVMRITDGLFAESCRNVLKGKVEYSEMYVDA
AAANLVRNPQAFDVIVTENTYGDILSDEAGQIAGSLGISPSANIGDRKSL
FEPVHGAAFDIAGKNIANPTAFLLSVGMMLDRMQELSGDIRYNNAAKSLR
DAIYSVYSEGKYLTPDVGGSSTTDEMISAIRSKIG
3D structure
PDB4y1p Characterization of two beta-decarboxylating dehydrogenases from Sulfolobus acidocaldarius
ChainA
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y124 K170 D201 D225 D229
Catalytic site (residue number reindexed from 1) Y122 K168 D199 D223 D227
Enzyme Commision number 1.1.1.85: 3-isopropylmalate dehydrogenase.
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 IPM A R86 R96 R117 Y124 D225 R85 R95 R115 Y122 D223
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0003862 3-isopropylmalate dehydrogenase activity
GO:0004449 isocitrate dehydrogenase (NAD+) activity
GO:0016491 oxidoreductase activity
GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
GO:0046872 metal ion binding
GO:0051287 NAD binding
Biological Process
GO:0006099 tricarboxylic acid cycle
GO:0006102 isocitrate metabolic process
GO:0009098 L-leucine biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:4y1p, PDBe:4y1p, PDBj:4y1p
PDBsum4y1p
PubMed27590116
UniProtQ4JB37

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