Structure of PDB 4qdp Chain A

Receptor sequence
>4qdpA (length=388) Species: 1929 (Streptomyces rubiginosus) [Search protein sequence]
MNYQPTPEDRFTFGLWTVGWQGRDPFGDATRRALDPVESVRRLAELGAHG
VTFHDDDLIPFGSSDSEREEHVKRFRQALDDTGMKVPMATTNLFTHPVFK
DGGFTANDRDVRRYALRKTIRNIDLAVELGAETYVAWGGREGAESGGAKD
VRDALDRMKEAFDLLGEYVTSQGYDIRFAIEPKPNEPRGDILLPTVGHAL
AFIERLERPELYGVNPEVGHEQMAGLNFPHGIAQALWAGKLFHIDLNGQN
GIKYDQDLRFGAGDLRAAFWLVDLLESAGYSGPRHFDFKPPRTEDFDGVW
ASAAGCMRNYLILKERAAAFRADPEVQEALRASRLDELARPTAADGLQAL
LDDRSAFEEFDVDAAAARGMAFERLDQLAMDHLLGARG
3D structure
PDB4qdp L-Arabinose Binding, Isomerization, and Epimerization by D-Xylose Isomerase: X-Ray/Neutron Crystallographic and Molecular Simulation Study.
ChainA
Resolution2.0 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 D255 D257 D287
Catalytic site (residue number reindexed from 1) H54 D57 M88 E181 K183 E217 H220 D245 D255 D257 D287
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 ARB A H54 F94 W137 E181 D287 H54 F94 W137 E181 D287
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: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:4qdp, PDBe:4qdp, PDBj:4qdp
PDBsum4qdp
PubMed25132082
UniProtP24300|XYLA_STRRU Xylose isomerase (Gene Name=xylA)

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