Structure of PDB 6n98 Chain A

Receptor sequence
>6n98A (length=379) Species: 463642 (Streptomyces sp. F-1) [Search protein sequence]
FQPTPEDRFCFGLWTVGWQERDQFGEATRAPLDPVRTVHKLAELGAWGVT
FHDDDLLAVEPNRDAAIAAFRKALDETGLVVPAATTDLFKHPVFKDGAFT
SNDRDVRRHAIRKVMRNLDLAAELGAKTYVFWGGREGAESDAAKDVRVAL
DRFREAIDYLAGYVKEQNYGMRFALEPKPNEPRGDILLPTIGHALGFIST
LEHHEMVGLNPEVGHEQMAGLNFVHGIAQALWQDKLFHIDLNGQHGPRYD
QDLVFGHGDTKSAFFLVDLLESSGWEGPRHFDYKPGRTEDAEDVWVSAEA
NMRTYLILKERAKAFRADPEVQEAMRACRIEELAVPTIAAGESYEDLRAE
EFDAEAARDRGYHYSRLNQLAVEHMLGSR
3D structure
PDB6n98 Crystal structure of a novel xylose isomerase from Streptomyces sp. F-1 revealed the presence of unique features that differ from conventional classes.
ChainA
Resolution1.55 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H55 D58 A86 E179 K181 E215 H218 D243 D253 D255 D285
Catalytic site (residue number reindexed from 1) H52 D55 A83 E176 K178 E212 H215 D240 D250 D252 D282
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 E179 E215 D243 D285 E176 E212 D240 D282
BS02 MG A E215 H218 D253 D255 E212 H215 D250 D252
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:6n98, PDBe:6n98, PDBj:6n98
PDBsum6n98
PubMed32035160
UniProtA0A1K2FZ20

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