Structure of PDB 1xyc Chain B

Receptor sequence
>1xycB (length=386) Species: 1963 (Streptomyces olivochromogenes) [Search protein sequence]
SYQPTPEDRFTFGLWTVGWQGRDPFGDATRPALDPVETVQRLAELGAHGV
TFHDDDLIPFGSSDTERESHIKRFRQALDATGMTVPMATTNLFTHPVFKD
GGFTANDRDVRRYALRKTIRNIDLAVELGAKTYVAWGGREGAESGAAKDV
RVALDRMKEAFDLLGEYVTSQGYDTRFAIEPKPNEPRGDILLPTVGHALA
FIERLERPELYGVNPEVGHEQMAGLNFPHGIAQALWAGKLFHIDLNGQSG
IKYDQDLRFGAGDLRAAFWLVDLLESAGYEGPRHFDFKPPRTEDIDGVWA
SAAGCMRNYLILKERAAAFRADPEVQEALRASRLDELAQPTAADGVQELL
ADRTAFEDFDVDAAAARGMAFERLDQLAMDHLLGAR
3D structure
PDB1xyc X-ray crystallographic structures of D-xylose isomerase-substrate complexes position the substrate and provide evidence for metal movement during catalysis.
ChainB
Resolution2.19 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H553 D556 M587 E680 K682 E716 H719 D744 D754 D756 D786
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 3MF B W515 H553 T589 W636 E680 K682 H719 D786 W15 H53 T89 W136 E180 K182 H219 D286
BS02 MG B E680 E716 D744 D786 E180 E216 D244 D286
BS03 MG B E716 H719 D754 D756 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:1xyc, PDBe:1xyc, PDBj:1xyc
PDBsum1xyc
PubMed8180169
UniProtP15587|XYLA_STROL Xylose isomerase (Gene Name=xylA)

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