Structure of PDB 4hhl Chain A

Receptor sequence
>4hhlA (length=386) Species: 253732 (Streptomyces sp. SK) [Search protein sequence]
NYQPTPEDRFTFGLWTVGWQGRDPFGDATRPALDPVEAVQRLAELGAYGV
TFHDDDLIPFGASDTEREAHVKRFRQALDATGMTVPMATTNLFTHPVFKD
GAFTANDRDVRRYALRKTIRNIDLAVELGAKVYVAWGGREGAESGAAKDV
RAALDRMKEAFDLLGEYVTSQGYDIRFAIEPKPNEPRGDILLPTIGHALA
FIERLERPELYGVNPEVGHEQMAGLNFPHGIAQALWAGKLFHIDLNGQSG
IKYDQDLRFGAGDLRAAFWLVDLLESAGWEGPRHFDFKPPRTEDIDGVWA
SAAGCMRNYLILKERAAAFRADPEVQEALRAARLDQLAEPTAADGLQALL
ADRTAYEDFDVDAAAARGMAFERLDQLAMDHLLGAR
3D structure
PDB4hhl Identification of critical residues for the activity and thermostability of Streptomyces sp. SK glucose isomerase.
ChainA
Resolution1.73 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 CO A E217 H220 D255 D257 E216 H219 D254 D256
BS02 MG A E181 E217 D245 D287 E180 E216 D244 D286
BS03 MG A E67 H71 E66 H70
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:4hhl, PDBe:4hhl, PDBj:4hhl
PDBsum4hhl
PubMed23463249
UniProtQ9ZAI3

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