Structure of PDB 7bjz Chain B

Receptor sequence
>7bjzB (length=386) Species: 1929 (Streptomyces rubiginosus) [Search protein sequence]
NYQPTPEDRFTFGLWTVGWQGRDPFGDATRRALDPVESVQRLAELGAHGV
TFHDDDLIPFGSSDSEREEHVKRFRQALDDTGMKVPMATTNLFTHPVFKD
GGFTANDRDVRRYALRKTIRNIDLAVELGAETYVAWGGREGAESGGAKDV
RDALDRMKEAFDLLGEYVTWQGYDIRFAIEPKPNEPRGDILLPTVGHALA
FIERLERPELYGVNPEVGHEQMAGLNFPHGIAQALWAGKLFHIDLNGQNG
IKYDQDLRFGAGDLRAAFWLVDLLESAGYSGPRHFDFKPPRTEDFDGVWA
SAAGCMRNYLILKERAAAFRADPEVQEALRASRLDELARPTAADGLQALL
DDRSAFEEFDVDAAAARGMAFERLDQLAMDHLLGAR
3D structure
PDB7bjz Nucleation of protein mesocrystals via oriented attachment.
ChainB
Resolution2.13 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) 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 MN B E217 H220 D255 D257 E216 H219 D254 D256
BS02 MN B E181 E217 D245 D287 E180 E216 D244 D286
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:7bjz, PDBe:7bjz, PDBj:7bjz
PDBsum7bjz
PubMed34162863
UniProtP24300|XYLA_STRRU Xylose isomerase (Gene Name=xylA)

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