Structure of PDB 1clk Chain A

Receptor sequence
>1clkA (length=387) Species: 1956 (Streptomyces diastaticus) [Search protein sequence]
SYQPTPEDKFTFGLWTVGWQGRDPFGDATRGALDPAESVRRLAELGAHGV
TFHDDDLIPFGATDSERAEHIKRFRQALDETGMKVPMATTNLFTHPVFKD
GGFTANDRDVRRYALRKTIRNIDLAVELGAQTYVAWGGREGAESGAAKDV
RVALDRMKEAFDLLGEYVTSQGYDTPFAIEPKPNEPRGDILLPTIGHALA
FIDGLERPELYGVNPEVGHEQMAGLNFPHGIAQALWAGKLFHIDLNGQSG
IKYDQDLRFGPGDLRAAFWLVDLLESAGYEGPRHFDFKPPRTEDFDGVWA
SAAGCMRNYLILKERAAAFRADPEVQEALRAARLDELAQPTAGDGLQALL
PDRSAFEDFDPDAAAARGMAFERLDQLAMDHLLGARG
3D structure
PDB1clk Structure of xylose isomerase from Streptomyces diastaticus no. 7 strain M1033 at 1.85 A resolution.
ChainA
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H53 D56 M87 E180 K182 E216 H219 D244 D254 D256 D286
Catalytic site (residue number reindexed from 1) H53 D56 M87 E180 K182 E216 H219 D244 D254 D256 D286
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 E180 E216 D244 D286 E180 E216 D244 D286
BS02 CO A E216 H219 D254 D256 E216 H219 D254 D256
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:1clk, PDBe:1clk, PDBj:1clk
PDBsum1clk
PubMed10666592
UniProtP50910|XYLA_STRDI Xylose isomerase (Gene Name=xylA)

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