Structure of PDB 1tyo Chain A

Receptor sequence
>1tyoA (length=427) Species: 56636 (Aeropyrum pernix) [Search protein sequence]
SPPCTTEELSPPPGGSLVEYSGGSLRVPDNPVVAFIRGDGVGPEVVESAL
KVVDAAVKKVYGGSRRIVWWELLAGHLAREKCGELLPKATLEGIRLARVA
LKGPLETPVGTGYRSLNVAIRQALDLYANIRPVRYYGQPAPHKYADRVDM
VIFRENTEDVYAGIEWPHDSPEAARIRRFLAEEFGISIREDAGIGVKPIS
RFATRRLMERALEWALRNGNTVVTIMHKGNIMKYTEGAFMRWAYEVALEK
FREHVVTEQEVQEKYGGVRPEGKILVNDRIADNMLQQIITRPWDYQVIVA
PNLNGDYISDAASALVGGIGMAAGMNMGDGIAVAEPVHGTAPKYAGKDLI
NPSAEILSASLLIGEFMGWREVKSIVEYAIRKAVQSKKVTQDLARHMPGV
QPLRTSEYTETLIAYIDEADLNEVLAG
3D structure
PDB1tyo Isocitrate dehydrogenase from the hyperthermophile Aeropyrum pernix: X-ray structure analysis of a ternary enzyme-substrate complex and thermal stability
ChainA
Resolution2.15 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y166 K233 D287 D311 D315
Catalytic site (residue number reindexed from 1) Y161 K228 D282 D306 D310
Enzyme Commision number 1.1.1.42: isocitrate dehydrogenase (NADP(+)).
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 ENP A D34 Y66 S69 R70 R375 E376 D29 Y61 S64 R65 R370 E371
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0000287 magnesium ion binding
GO:0004450 isocitrate dehydrogenase (NADP+) 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:0006097 glyoxylate cycle
GO:0006099 tricarboxylic acid cycle

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Molecular Function
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Biological Process
External links
PDB RCSB:1tyo, PDBe:1tyo, PDBj:1tyo
PDBsum1tyo
PubMed15581899
UniProtQ9YE81

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