Structure of PDB 2exi Chain A

Receptor sequence
>2exiA (length=533) Species: 1422 (Geobacillus stearothermophilus) [Search protein sequence]
KIKNPILTGFHPGPSICRVGDDYYIAVSTFEWFPGVRIYHSKDLKNWRLV
ARPLNRLSQLNMIGNPDSGGVWAPHLSYSDGKFWLIYTDVKVVEGQWKDG
HNYLVTCDTIDGAWSDPIYLNSSGFDPSLFHDEDGRKYLVNMYWDHRVDH
HPFYGIVLQEYSVEQKKLVGEPKIIFKGTDLRITEGPHLYKINGYYYLLT
AEGGTRYNHAATIARSTSLYGPYEVHPDNPLLTSWPYPRNPLQKAGHASI
VHTHTDEWFLVHLTGRPLPREGQPLLEHRGYCPLGRETAIQRLEWKDGWP
YVVGGNGPSLEIDGPSVEEVSWEKDYDEKDDFDGDTLNHHFQTLRIPLGE
DIATLKARPGHLRLYGRESLTSRFTQAFVARRWQHFHFVAETKVSFRPTT
FQQSAGLVNYYNTQNWTTLQITWHEEKGRILELMTCDHLVVDQPLRGREI
VVPDDIEYVYLRVTVQATTYKYSYSFDGMNWIDLPVTFESYKLSDDYIKS
RAAFTGAFVGMHCRDGSGQNNYADFDYFLYKEL
3D structure
PDB2exi The Structure of an Inverting GH43 beta-Xylosidase from Geobacillus stearothermophilus with its Substrate Reveals the Role of the Three Catalytic Residues.
ChainA
Resolution2.15 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 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

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Molecular Function
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Biological Process
External links
PDB RCSB:2exi, PDBe:2exi, PDBj:2exi
PDBsum2exi
PubMed16631196
UniProtQ09LX0

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