Structure of PDB 7cjo Chain B Binding Site BS02
Receptor Information
>7cjo Chain B (length=386) Species:
1929
(Streptomyces rubiginosus) [
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NYQPTPEDRFTFGLWTVGWQGRDPFGDATRRALDPVESVRRLAELGAHGV
TFHDDDLIPFGSSDSEREEHVKRFRQALDDTGMKVPMATTNLFTHPVFKD
GGFTANDRDVRRYALRKTIRNIDLAVELGAETYVAWGGREGAESGGAKDV
RDALDRMKEAFDLLGEYVTSQGYDIRFAIEPKPNEPRGDILLPTVGHALA
FIERLERPELYGVNPEVGHEQMAGLNFPHGIAQALWAGKLFHIDLNGQNG
IKYDQDLRFGAGDLRAAFWLVDLLESAGYSGPRHFDFKPPRTEDFDGVWA
SAAGCMRNYLILKERAAAFRADPEVQEALRASRLDELARPTAADGLQALL
DDRSAFEEFDVDAAAARGMAFERLDQLAMDHLLGAR
Ligand information
Ligand ID
MG
InChI
InChI=1S/Mg/q+2
InChIKey
JLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mg+2]
CACTVS 3.341
[Mg++]
Formula
Mg
Name
MAGNESIUM ION
ChEMBL
DrugBank
DB01378
ZINC
PDB chain
7cjo Chain B Residue 1212 [
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Receptor-Ligand Complex Structure
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PDB
7cjo
Crystal structure of the metal-free state of glucose isomerase reveals its minimal open configuration for metal binding.
Resolution
1.4 Å
Binding residue
(original residue number in PDB)
E217 H220 D255 D257
Binding residue
(residue number reindexed from 1)
E216 H219 D254 D256
Annotation score
1
Enzymatic activity
Enzyme Commision number
5.3.1.5
: xylose isomerase.
Gene Ontology
Molecular Function
GO:0000287
magnesium ion binding
GO:0009045
xylose isomerase activity
GO:0016853
isomerase activity
GO:0042802
identical protein binding
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:7cjo
,
PDBe:7cjo
,
PDBj:7cjo
PDBsum
7cjo
PubMed
33610042
UniProt
P24300
|XYLA_STRRU Xylose isomerase (Gene Name=xylA)
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