Structure of PDB 5nh6 Chain D

Receptor sequence
>5nh6D (length=435) Species: 73868 (Piromyces sp. E2) [Search protein sequence]
KEYFPQIQKIKFEGKDSKNPLAFHYYDAEKEVMGKKMKDWLRFAMAWWHT
LCAEGADQFGGGTKSFPWNEGTDAIEIAKQKVDAGFEIMQKLGIPYYCFH
DVDLVSEGNSIEEYESNLKAVVAYLKEKQKETGIKLLWSTANVFGHKRYM
NGASTNPDFDVVARAIVQIKNAIDAGIELGAENYVFWGGREGYMSLLNTD
QKREKEHMATMLTMARDYARSKGFKGTFLIEPKPMEPTKHQYDVDTETAI
GFLKAHNLDKDFKVNIEVNHATLAGHTFEHELACAVDAGMLGSIDANRGD
YQNGWDTDQFPIDQYELVQAWMEIIRGGGFVTGGTNFDAKTRRNSTDLED
IIIAHVSGMDAMARALENAAKLLQESPYTKMKKERYASFDSGIGKDFEDG
KLTLEQVYEYGKKNGEPKQTSGKQELYEAIVAMYQ
3D structure
PDB5nh6 Metal Dependence of the Xylose Isomerase from Piromyces sp. E2 Explored by Activity Profiling and Protein Crystallography.
ChainD
Resolution1.75 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H102 D105 W140 E233 K235 E269 H272 D297 D308 D310 D340
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 MG D E233 E269 D297 D340 E231 E267 D295 D338
BS02 XYL D H102 W189 E233 E269 H272 D340 H100 W187 E231 E267 H270 D338
Gene Ontology
Molecular Function
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
GO:0044577 D-xylose catabolic process to ethanol

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Molecular Function
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Biological Process
External links
PDB RCSB:5nh6, PDBe:5nh6, PDBj:5nh6
PDBsum5nh6
PubMed29045784
UniProtQ9P8C9

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