Structure of PDB 1dxi Chain A

Receptor sequence
>1dxiA (length=388) Species: 33900 (Streptomyces murinus) [Search protein sequence]
MSFQPTPEDRFTFGLWTVGWQGRDPFGDATRPALDPVETVQRLAELGAYG
VTFHDDDLIPFGSSDTERESHIKRFRQALDATGMTVPMATTNLFTHPVFK
DGGFTANDRDVRRYALRKTIGNIDLAAELGAKTYVAWGGREGAESGGAKD
VRDALDRMKEAFDLLGEYVTAQGYDLRFAIEPKPNEPRGDILLPTVGHAL
AFIERLERPELYGVNPEVGHEQMAGLNFPHGIAQALWAGKLFHIDLNGQS
GIKYDQDLRFGAGDLRAAFWLVDLLETAGYEGPRHFDFKPPRTEDFDGVW
ASAAGCMRNYLILKDRAAAFRADPEVQEALRAARLDQLAQPTAADGLDAL
LADRAAFEDFDVDAAAARGMAFEHLDQLAMDHLLGARG
3D structure
PDB1dxi Structure determination of glucose isomerase from Streptomyces murinus at 2.6 A resolution.
ChainA
Resolution2.6 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) H54 D57 M88 E181 K183 E217 H220 D245 D255 D257 D287
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 E181 E217 D245 D287 E181 E217 D245 D287
BS02 MG A E217 H220 D255 D257 E217 H220 D255 D257
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:1dxi, PDBe:1dxi, PDBj:1dxi
PDBsum1dxi
PubMed15299450
UniProtP37031|XYLA_STRMR Xylose isomerase (Gene Name=xylA)

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