Structure of PDB 7ch3 Chain D

Receptor sequence
>7ch3D (length=495) Species: 243274 (Thermotoga maritima MSB8) [Search protein sequence]
MIDLKQYEFWFLVGSQYLYGLETLKKVEQQASKIVDSLNDDPIFPSKIVL
KPVLKSSSEITEIFEKANADPKCAGVIVWMHTFSPSKMWIRGLSINKKPL
LHLHTQYNREIPWDTIDMDYMNLNQSAHGDREHGFIHARMRLPRKVVVGH
WEEKEVREKIAKWMRVACAIQDGRMGQIVRFGDNMREVASTEGDKVEAQI
KLGWSINTWGVGELAERVKAVPEREVEELLKEYREKYIMPEDEYSLKAIR
EQAKIEIALREFLAAANAVGFTTTFEDLHDLPQLPGLAVQRLMEEGYGFG
AEGDWKAAGLVRAIKVMGTSLPGGTSFMEDYTYHLTPGNELVLGAHMLEV
CPTIAKEKPRIEVHPLSIGGKADPARLVFDGQEGPAVNASIVDMGNRFRL
VVNKVLSVPIERKMPKLPTARVLWKPLPDFKRATTAWILAGGSHHTAFST
AIDVEYLIDWAEALEIEYVVIDENLDLEDFKKELRWNELYWGLLK
3D structure
PDB7ch3 Crystal structure of Arabinose isomerase from hyper thermophilic bacterium Thermotoga maritima (TMAI) triple mutant (K264A, E265A, K266A)
ChainD
Resolution3.61 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 5.3.1.4: L-arabinose isomerase.
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 MN D D194 E197 G395 D194 E197 G395
BS02 MN D E302 E329 H445 E302 E329 H445
Gene Ontology
Molecular Function
GO:0008733 L-arabinose isomerase activity
GO:0016853 isomerase activity
GO:0016861 intramolecular oxidoreductase activity, interconverting aldoses and ketoses
GO:0030145 manganese ion binding
GO:0046872 metal ion binding
Biological Process
GO:0005996 monosaccharide metabolic process
GO:0019568 arabinose catabolic process
GO:0019569 L-arabinose catabolic process to xylulose 5-phosphate
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:7ch3, PDBe:7ch3, PDBj:7ch3
PDBsum7ch3
PubMed
UniProtQ9WYB3|ARAA_THEMA L-arabinose isomerase (Gene Name=araA)

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