Structure of PDB 6n99 Chain A

Receptor sequence
>6n99A (length=384) Species: 463642 (Streptomyces sp. F-1) [Search protein sequence]
YQPTPEDRFTFGLWTVGWQGRDPFGDATRRALDPVETVQRLAELGAHGVT
FHDDDLIPFGSSDAEREAHIKRFREALDATGMKVPMATTNLFTHPVFKDG
GFTANDRDVRRYALRKTIRNIDLAAELGAEVYVAWGGREGAESGAAKDVR
AALDRMKEAFDILGEYVTAQGYNLRFAIEPKPNEPRGDILLPTVGHALAF
IERLERPELYGVNPEVGHEQMAGLNFPHGIAQALWAGKLFHIDLNGQSGI
KYDQDLRFGAGDLRAAFWLVDLLESAGYEGPRHFDFKPPRTEDLDGVWAS
AAGCMRNYLILKERSAAFRADPEVQEALRAARLDQLAEPTAADGLQALLA
DRTAFEDFDVDAAAARGMAFERLDQLAMDHLLGA
3D structure
PDB6n99 Crystal structure of a novel xylose isomerase from Streptomyces sp. F-1 revealed the presence of unique features that differ from conventional classes.
ChainA
Resolution2.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H54 D57 M88 E181 K183 E217 H220 D245 D255 D257 D287
Catalytic site (residue number reindexed from 1) H52 D55 M86 E179 K181 E215 H218 D243 D253 D255 D285
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 A E217 H220 D255 D257 E215 H218 D253 D255
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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Cellular Component
External links
PDB RCSB:6n99, PDBe:6n99, PDBj:6n99
PDBsum6n99
PubMed32035160
UniProtA0A1K2FKX8

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