Structure of PDB 2exj Chain A

Receptor sequence
>2exjA (length=533) Species: 1422 (Geobacillus stearothermophilus) [Search protein sequence]
KIKNPILTGFHPDPSICRVGDDYYIAVSTFEWFPGVRIYHSKDLKNWRLV
ARPLNRLSQLNMIGNPDSGGVWAPHLSYSDGKFWLIYTDVKVVEGQWKDG
HNYLVTCDTIDGAWSDPIYLNSSGFGPSLFHDEDGRKYLVNMYWDHRVDH
HPFYGIVLQEYSVEQKKLVGEPKIIFKGTDLRITEGPHLYKINGYYYLLT
AEGGTRYNHAATIARSTSLYGPYEVHPDNPLLTSWPYPRNPLQKAGHASI
VHTHTDEWFLVHLTGRPLPREGQPLLEHRGYCPLGRETAIQRLEWKDGWP
YVVGGNGPSLEIDGPSVEEVSWEKDYDEKDDFDGDTLNHHFQTLRIPLGE
DIATLKARPGHLRLYGRESLTSRFTQAFVARRWQHFHFVAETKVSFRPTT
FQQSAGLVNYYNTQNWTTLQITWHEEKGRILELMTCDHLVVDQPLRGREI
VVPDDIEYVYLRVTVQATTYKYSYSFDGMNWIDLPVTFESYKLSDDYIKS
RAAFTGAFVGMHCRDGSGQNNYADFDYFLYKEL
3D structure
PDB2exj The Structure of an Inverting GH43 beta-Xylosidase from Geobacillus stearothermophilus with its Substrate Reveals the Role of the Three Catalytic Residues.
ChainA
Resolution2.2 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.2.1.37: xylan 1,4-beta-xylosidase.
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 XYS A W74 E187 G206 W72 E185 G204
BS02 XYS A D15 F32 W74 A75 E187 H249 R288 F506 D13 F30 W72 A73 E185 H247 R286 F504
BS03 CA A D333 G362 D528 D331 G360 D526
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
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Biological Process
External links
PDB RCSB:2exj, PDBe:2exj, PDBj:2exj
PDBsum2exj
PubMed16631196
UniProtQ09LX0

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