Structure of PDB 2exk Chain D Binding Site BS02

Receptor Information
>2exk Chain D (length=533) Species: 1422 (Geobacillus stearothermophilus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KIKNPILTGFHPDPSICRVGDDYYIAVSTFEWFPGVRIYHSKDLKNWRLV
ARPLNRLSQLNMIGNPDSGGVWAPHLSYSDGKFWLIYTDVKVVEGQWKDG
HNYLVTCDTIDGAWSDPIYLNSSGFDPSLFHDEDGRKYLVNMYWDHRVDH
HPFYGIVLQEYSVEQKKLVGEPKIIFKGTDLRITGGPHLYKINGYYYLLT
AEGGTRYNHAATIARSTSLYGPYEVHPDNPLLTSWPYPRNPLQKAGHASI
VHTHTDEWFLVHLTGRPLPREGQPLLEHRGYCPLGRETAIQRLEWKDGWP
YVVGGNGPSLEIDGPSVEEVSWEKDYDEKDDFDGDTLNHHFQTLRIPLGE
DIATLKARPGHLRLYGRESLTSRFTQAFVARRWQHFHFVAETKVSFRPTT
FQQSAGLVNYYNTQNWTTLQITWHEEKGRILELMTCDHLVVDQPLRGREI
VVPDDIEYVYLRVTVQATTYKYSYSFDGMNWIDLPVTFESYKLSDDYIKS
RAAFTGAFVGMHCRDGSGQNNYADFDYFLYKEL
Ligand information
Ligand IDXYS
InChIInChI=1S/C5H10O5/c6-2-1-10-5(9)4(8)3(2)7/h2-9H,1H2/t2-,3+,4-,5+/m1/s1
InChIKeySRBFZHDQGSBBOR-LECHCGJUSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0C1C(C(C(C(O1)O)O)O)O
CACTVS 3.341O[CH]1CO[CH](O)[CH](O)[CH]1O
OpenEye OEToolkits 1.5.0C1[C@H]([C@@H]([C@H]([C@H](O1)O)O)O)O
CACTVS 3.341O[C@@H]1CO[C@H](O)[C@H](O)[C@H]1O
ACDLabs 10.04OC1C(O)COC(O)C1O
FormulaC5 H10 O5
Namealpha-D-xylopyranose;
alpha-D-xylose;
D-xylose;
xylose;
XYLOPYRANOSE
ChEMBL
DrugBankDB03389
ZINCZINC000001529214
PDB chain2exk Chain H Residue 2 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2exk The Structure of an Inverting GH43 beta-Xylosidase from Geobacillus stearothermophilus with its Substrate Reveals the Role of the Three Catalytic Residues.
Resolution2.2 Å
Binding residue
(original residue number in PDB)		D15 F32 W74 A75 F127 D128 R288 F506
Binding residue
(residue number reindexed from 1)		D13 F30 W72 A73 F125 D126 R286 F504
Annotation score4
Enzymatic activity
Enzyme Commision number 3.2.1.37: xylan 1,4-beta-xylosidase.
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0046872 metal ion binding
Biological Process
GO:0005975 carbohydrate metabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:2exk, PDBe:2exk, PDBj:2exk
PDBsum2exk
PubMed16631196
UniProtQ09LX0

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