Structure of PDB 1a0c Chain D

Receptor sequence
>1a0cD (length=437) Species: 33950 (Thermoanaerobacterium thermosulfurigenes) [Search protein sequence]
NKYFENVSKIKYEGPKSNNPYSFKFYNPEEVIDGKTMEEHLRFSIAYWHT
FTADGTDQFGKATMQRPWNHYTDPMDIAKARVEAAFEFFDKINAPYFCFH
DRDIAPEGDTLRETNKNLDTIVAMIKDYLKTSKTKVLWGTANLFSNPRFV
HGASTSCNADVFAYSAAQVKKALEITKELGGENYVFWGGREGYETLLNTD
MEFELDNFARFLHMAVDYAKEIGFEGQFLIEPKPKEPTKHQYDFDVANVL
AFLRKYDLDKYFKVNIEANHATLAFHDFQHELRYARINGVLGSIDANTGD
MLLGWDTDQFPTDIRMTTLAMYEVIKMGGFDKGGLNFDAKVRRASFEPED
LFLGHIAGMDAFAKGFKVAYKLVKDRVFDKFIEERYASYKDGIGADIVSG
KADFRSLEKYALERSQIVNKSGRQELLESILNQYLFA
3D structure
PDB1a0c Catalytic Mechanism of Xylose (Glucose) Isomerase from Clostridium Thermosulfurogenes. Characterization of the Structural Gene and Function of Active Site Histidine
ChainD
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H100 D103 W138 E231 K233 E267 H270 D295 D306 D308 D338
Catalytic site (residue number reindexed from 1) H100 D103 W138 E231 K233 E267 H270 D295 D306 D308 D338
Enzyme Commision number 5.3.1.5: xylose 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 CO D E231 E267 D295 D338 E231 E267 D295 D338
BS02 CO D E267 H270 D306 D308 E267 H270 D306 D308
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0009045 xylose isomerase activity
GO:0016853 isomerase activity
GO:0046872 metal ion binding
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0042732 D-xylose metabolic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1a0c, PDBe:1a0c, PDBj:1a0c
PDBsum1a0c
PubMed
UniProtP19148|XYLA_THETU Xylose isomerase (Gene Name=xylA)

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