Structure of PDB 1xin Chain B

Receptor sequence
>1xinB (length=392) Species: 1866 (Actinoplanes missouriensis) [Search protein sequence]
VQATREDKFSFGLWTVGWQARDAFGDATRTALDPVEAVHKLAEIGAYGIT
FHDDDLVPFGSDAQTRDGIIAGFKKALDETGLIVPMVTTNLFTHPVFKDG
GFTSNDRSVRRYAIRKVLRQMDLGAELGAKTLVLWGGREGAEYDSAKDVS
AALDRYREALNLLAQYSEDRGYGLRFAIEPKPNEPRGDILLPTAGHAIAF
VQELERPELFGINPETGNEQMSNLNFTQGIAQALWHKKLFHIDLNGQHGP
KFDQDLVFGHGDLLNAFSLVDLLENGPDGAPAYDGPRHFDYKPSRTEDYD
GVWESAKANIRMYLLLKERAKAFRADPEVQEALAASKVAELKTPTLNPGE
GYAELLADRSAFEDYDADAVGAKGFGFVKLNQLAIEHLLGAR
3D structure
PDB1xin Protein engineering of xylose (glucose) isomerase from Actinoplanes missouriensis. 1. Crystallography and site-directed mutagenesis of metal binding sites.
ChainB
Resolution2.4 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 N220 D245 D255 D257 D292
Catalytic site (residue number reindexed from 1) H52 D55 M86 E179 K181 E215 N218 D243 D253 D255 D290
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 XYL B H54 W137 E181 K183 D292 H52 W135 E179 K181 D290
BS02 MG B E181 E217 D245 D292 E179 E215 D243 D290
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:1xin, PDBe:1xin, PDBj:1xin
PDBsum1xin
PubMed1610791
UniProtP12851|XYLA_ACTM4 Xylose isomerase (Gene Name=xylA)

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