Structure of PDB 2bfg Chain A

Receptor sequence
>2bfgA (length=501) Species: 1422 (Geobacillus stearothermophilus) [Search protein sequence]
GVVNVPSNGREKFKKNWKFCVGTGRLGLALQKEYLDHLKLVQEKIGFRYI
RGHGLLSDDVGIYREVEIDGEMKPFYNFTYIDRIVDSYLALNIRPFIEFG
FMPKALASGDQTVFYWKGNVTPPKDYNKWRDLIVAVVSHFIERYGIEEVR
TWLFEVWNAPNLVNFWKDANKQEYFKLYEVTARAVKSVDPHLQVGGPAIC
GGSDEWITDFLHFCAERRVPVDFVSRHAYTSKAPHKKTFEYYYQELEPPE
DMLEQFKTVRALIRQSPFPHLPLHITEYNTSYSPINPVHDTALNAAYIAR
ILSEGGDYVDSFSYWTFSDVFEEMDVPKALFHGGFGLVALHSIPKPTFHA
FTFFNALGDELLYRDGEMIVTRRKDGSIAAVLWNLVMEKGEGLTKEVQLV
IPVSESAVFIKRQIVNEQYGNAWRVWKQMGRPRFPSRQAVETLRQVAQPH
VMTEQRRATDGVIHLSIVLSKNEVTLIEIEQVRDETSTYVGLDDGEITSY
S
3D structure
PDB2bfg Enzyme-Substrate Complex Structures of a Gh39 Beta-Xylosidase from Geobacillus Stearothermophilus.
ChainA
Resolution2.4 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 ANX A L163 F166 C201 Y283 L162 F165 C200 Y282
BS02 XYP A H54 N159 F166 Y230 E278 W316 E324 F336 H53 N158 F165 Y229 E277 W315 E323 F335
BS03 XYS A H54 N159 Y230 E278 W316 E324 F336 H53 N158 Y229 E277 W315 E323 F335
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
Biological Process
GO:0005975 carbohydrate metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:2bfg, PDBe:2bfg, PDBj:2bfg
PDBsum2bfg
PubMed16212978
UniProtQ9ZFM2|XYNB_GEOSE Beta-xylosidase (Gene Name=xynB)

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