2BVD: Endoglucanase H

How family 26 glycoside hydrolases orchestrate catalysis on different polysaccharides. Structure and activity of a clostridium thermocellum lichenase, CtLIC26A. Determined by X-ray diffraction at 1.6 Å resolution. Released 30 Jun 2005.

Method
X-ray diffraction
Resolution
1.6 Å
Organism
CLOSTRIDIUM THERMOCELLUM
Chains
1
Atoms
2,721
Mol. weight
32.54 kDa
Ligands
ISX
Released
30 Jun 2005

Explore 2BVD in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2BVD contains 9 α-helices and 13 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 9 helices, 13 β-strands

ElementResiduesLengthSheet
β-strand10-1451
α-helix21-3111
β-strand37-4371
α-helix48-6013
β-strand64-7071
α-helix76-805
α-helix85-9814
β-strand102-10651
α-helix128-14417
β-strand150-15231
β-strand15312
β-strand156-15721
α-helix174-1763
β-strand17912
β-strand180-18671
α-helix200-21112
β-strand218-22581
α-helix232-24615
β-strand250-25671
β-strand25913
β-strand26313
α-helix270-28011

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Endoglucanase HAprotein283CLOSTRIDIUM THERMOCELLUMP16218 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2BVD_1 ENDOGLUCANASE H (chains A)
MASNYNSGLKIGAWVGTQPSESAIKSFQELQGRKLDIVHQFINWSTDFSWVRPYADAVYN
NGSILMITWEPWEYNTVDIKNGKADAYITRMAQDMKAYGKEIWLRPLHEANGDWYPWAIG
YSSRVNTNETYIAAFRHIVDIFRANGATNVKWVFNVNCDNVGNGTSYLGHYPGDNYVDYT
SIDGYNWGTTQSWGSQWQSFDQVFSRAYQALASINKPIIIAEFASAEIGGNKARWITEAY
NSIRTSYNKVIAAVWFHENKETDWRINSSPEALAAYREAIGAL

Ligands and cofactors

IDNameFormulaCopies
ISX(3R,4R,5R)-4-hydroxy-5-(hydroxymethyl)piperidin-3-yl beta-D-glucopyranosideC12 H23 N O81

Primary citation

How Family 26 Glycoside Hydrolases Orchestrate Catalysis on Different Polysaccharides: Structure and Activity of a Clostridium Thermocellum Lichenase, Ctlic26A. Taylor, E.J., Goyal, A., Guerreiro, C.I.P.D. et al. J Biol Chem (2005) 280:32761. DOI 10.1074/JBC.M506580200 · PubMed

Other PDB entries of the same protein (UniProt P16218 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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