Structure of PDB 4hhl Chain B

Receptor sequence
>4hhlB (length=385) Species: 253732 (Streptomyces sp. SK) [Search protein sequence]
YQPTPEDRFTFGLWTVGWQGRDPFGDATRPALDPVEAVQRLAELGAYGVT
FHDDDLIPFGASDTEREAHVKRFRQALDATGMTVPMATTNLFTHPVFKDG
AFTANDRDVRRYALRKTIRNIDLAVELGAKVYVAWGGREGAESGAAKDVR
AALDRMKEAFDLLGEYVTSQGYDIRFAIEPKPNEPRGDILLPTIGHALAF
IERLERPELYGVNPEVGHEQMAGLNFPHGIAQALWAGKLFHIDLNGQSGI
KYDQDLRFGAGDLRAAFWLVDLLESAGWEGPRHFDFKPPRTEDIDGVWAS
AAGCMRNYLILKERAAAFRADPEVQEALRAARLDQLAEPTAADGLQALLA
DRTAYEDFDVDAAAARGMAFERLDQLAMDHLLGAR
3D structure
PDB4hhl Identification of critical residues for the activity and thermostability of Streptomyces sp. SK glucose isomerase.
ChainB
Resolution1.73 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 CO B E217 H220 D255 D257 E215 H218 D253 D255
BS02 MG B E181 E217 D245 D287 E179 E215 D243 D285
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:4hhl, PDBe:4hhl, PDBj:4hhl
PDBsum4hhl
PubMed23463249
UniProtQ9ZAI3

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