Structure of PDB 5xin Chain D

Receptor sequence
>5xinD (length=392) Species: 1866 (Actinoplanes missouriensis) [Search protein sequence]
VQATREDKFSFGLWTVGWQARDAFGDATRTALDPVEAVHKLAEIGAYGIT
FHDDDLVPFGSDAQTRDGIIAGFKKALDETGLIVPMVTTNLFTHPVFKDG
GFTSNDRSVRRYAIRKVLRQMDLGAELGAKTLVLWGGREGAEYDSAKDVS
AALDRYREALNLLAQYSEDRGYGLRFAIEPKPNEPRGDILLPTAGHAIAF
VQELERPELFGINPETGHEQMSNLNFTQGIAQALWHKKLFHIDLNGQHGP
KFAQDLVFGHGDLLNAFSLVDLLENGPDGAPAYDGPRHFDYKPSRTEDYD
GVWESAKANIRMYLLLKERAKAFRADPEVQEALAASKVAELKTPTLNPGE
GYAELLADRSAFEDYDADAVGAKGFGFVKLNQLAIEHLLGAR
3D structure
PDB5xin Protein engineering of xylose (glucose) isomerase from Actinoplanes missouriensis. 1. Crystallography and site-directed mutagenesis of metal binding sites.
ChainD
Resolution2.3 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 A255 D257 D292
Catalytic site (residue number reindexed from 1) H52 D55 M86 E179 K181 E215 H218 D243 A253 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 XLS D H54 W137 E181 H220 D292 H52 W135 E179 H218 D290
BS02 MG D 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:5xin, PDBe:5xin, PDBj:5xin
PDBsum5xin
PubMed1610791
UniProtP12851|XYLA_ACTM4 Xylose isomerase (Gene Name=xylA)

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