Structure of PDB 3aoe Chain E

Receptor sequence
>3aoeE (length=416) Species: 262724 (Thermus thermophilus HB27) [Search protein sequence]
KAYRPPEDPGLWDTYLEWLERALKVAGVHPTTLEYLAHPKRLVTLSLPVV
MDDGKVRIFQGYRVVHDIARGPAKGGVRLDPGVTLGQTAGLAAWMTLKAA
VYDLPFGGAAGGIAVDPKGLSPQELERLVRRYTAELVGLIGPDSDILGPD
LGADQQVMAWIMDTYSMTVGSTVPGVVTGKPHALGGSEGRDDAAGLGALL
VLEALAKRRGLDLRGARVVVQGLGQVGAAVALHAERLGMRVVAVATSMGG
MYAPEGLDVAEVLSAYEATGSLPRLDLAPEEVFGLEAEVLVLAAREGALD
GDRARQVQAQAVVEVANFGLNPEAEAYLLGKGALVVPDLLSGGGGLLASY
LEWVQDLNMFFWSPEEVRERFETRVARVVDAVCRRAERGGLDLRMGALAL
ALERLDEATRLRGVYP
3D structure
PDB3aoe An unique allosteric regulation revealed by hetero-hexameric glutamate dehydrogenase from Thermus thermophilus
ChainE
Resolution2.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) A113 D153
Catalytic site (residue number reindexed from 1) A110 D150
Enzyme Commision number 1.4.1.3: glutamate dehydrogenase [NAD(P)(+)].
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 LEU E Y38 G416 V417 Y418 Y35 G413 V414 Y415
BS02 LEU E D166 M170 D163 M167
Gene Ontology
Molecular Function
GO:0004352 glutamate dehydrogenase (NAD+) activity
GO:0016491 oxidoreductase activity
GO:0016639 oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor
Biological Process
GO:0006520 amino acid metabolic process
GO:0006538 glutamate catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3aoe, PDBe:3aoe, PDBj:3aoe
PDBsum3aoe
PubMed
UniProtQ72IC0

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