Structure of PDB 5nhc Chain D

Receptor sequence
>5nhcD (length=436) Species: 73868 (Piromyces sp. E2) [Search protein sequence]
AKEYFPQIQKIKFEGKDSKNPLAFHYYDAEKEVMGKKMKDWLRFAMAWWH
TLCAEGADQFGGGTKSFPWNEGTDAIEIAKQKVDAGFEIMQKLGIPYYCF
HDVDLVSEGNSIEEYESNLKAVVAYLKEKQKETGIKLLWSTANVFGHKRY
MNGASTNPDFDVVARAIVQIKNAIDAGIELGAENYVFWGGREGYMSLLNT
DQKREKEHMATMLTMARDYARSKGFKGTFLIEPKPMEPTKHQYDVDTETA
IGFLKAHNLDKDFKVNIEVNHATLAGHTFEHELACAVDAGMLGSIDANRG
DYQNGWDTDQFPIDQYELVQAWMEIIRGGGFVTGGTNFDAKTRRNSTDLE
DIIIAHVSGMDAMARALENAAKLLQESPYTKMKKERYASFDSGIGKDFED
GKLTLEQVYEYGKKNGEPKQTSGKQELYEAIVAMYQ
3D structure
PDB5nhc Metal Dependence of the Xylose Isomerase from Piromyces sp. E2 Explored by Activity Profiling and Protein Crystallography.
ChainD
Resolution1.93 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) H101 D104 W139 E232 K234 E268 H271 D296 D307 D309 D339
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 E233 E269 D297 D340 E232 E268 D296 D339
BS02 CO D E269 H272 D308 D310 E268 H271 D307 D309
BS03 XUL D W50 H102 W189 E233 E269 H272 D340 W49 H101 W188 E232 E268 H271 D339
BS04 HYP D G291 L293 G329 G331 V333 G290 L292 G328 G330 V332
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

View graph for
Biological Process
External links
PDB RCSB:5nhc, PDBe:5nhc, PDBj:5nhc
PDBsum5nhc
PubMed29045784
UniProtQ9P8C9

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