Structure of PDB 2bog Chain X

Receptor sequence
>2bogX (length=280) Species: 2021 (Thermobifida fusca) [Search protein sequence]
NDSPFYVNPNMSSAEWVRNNPNDPRTPVIRDRIASVPQGTWFAHHNPGQI
TGQVDALMSAAQAAGKIPILVVSNAPGRDCGAPSHSAYRSWIDEFAAGLK
NRPAYIIVEPDLISLMSSCMQHVQQEVLETMAYAGKALKAGSSQARIYFD
AGHSAWHSPAQMASWLQQADISNSAHGIATNTSNYRWTADEVAYAKAVLS
AIGNPSLRAVIDTSRNGNGPAGNEWCDPSGRAIGTPSTTNTGDPMIDAFL
WIKLPGEADGCIAGAGQFVPQAAYEMAIAA
3D structure
PDB2bog Crystal Structure of Thermobifida Fusca Endoglucanase Cel6A in Complex with Substrate and Inhibitor: The Role of Tyrosine Y73 in Substrate Ring Distortion.
ChainX
Resolution1.04 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D117
Catalytic site (residue number reindexed from 1) D111
Enzyme Commision number 3.2.1.4: cellulase.
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 MGL X H159 W162 H153 W156
BS02 SGC X D117 H159 N190 W231 D111 H153 N184 W225
BS03 BGC X W231 K259 D265 W225 K253 D259
BS04 BGC X W41 K259 E263 A271 W41 K253 E257 A265
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0030245 cellulose catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:2bog, PDBe:2bog, PDBj:2bog
PDBsum2bog
PubMed16185060
UniProtP26222|GUN2_THEFU Endoglucanase E-2 (Gene Name=celB)

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