1C5H: Endo-1,4-beta-xylanase

Hydrogen bonding and catalysis: an unexpected explanation for how a single amino acid substitution can change the PH optimum of a glycosidase. Determined by X-ray diffraction at 1.55 Å resolution. Released 12 May 2000.

Method: X-ray diffraction
Resolution: 1.55 Å
Organism: Bacillus circulans
Chains: 1
Atoms: 1,594
Mol. weight: 20.41 kDa
Released: 12 May 2000

Explore 1C5H in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1C5H contains 3 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: 3 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	5-10	6	1
β-strand	15-20	6	2
β-strand	25-31	7	2
β-strand	35-42	8	1
β-strand	50-61	12	2
β-strand	64-73	10	1
β-strand	77-85	9	1
β-strand	93-100	8	1
β-strand	103-116	14	1
β-strand	122-132	11	1
α-helix	135-137	3
β-strand	142-145	4	2
α-helix	146-155	10
α-helix	159-161	3
β-strand	163-174	12	1
β-strand	177-184	8	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Endo-1,4-beta-xylanase	A	protein	185	Bacillus circulans	P09850 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1C5H_1 ENDO-1,4-BETA-XYLANASE (chains A)
ASTDYWQNWTDGGGIVNAVNGSGGNYSVNWSNTGDFVVGKGWTTGSPFRTINYNAGVWAP
NGNGYLTLYGWTRSPLIEYYVVDSWGTYRPTGTYKGTVKSDGGTYDIYTTTRYNAPSIDG
DRTTFTQYWSVRQSKRPTGSNATITFTNHVNAWKSHGMNLGSNWAYQVMATEGYQSSGSS
NVTVW

Primary citation

Hydrogen bonding and catalysis: a novel explanation for how a single amino acid substitution can change the pH optimum of a glycosidase. Joshi, M.D., Sidhu, G., Pot, I. et al. J Mol Biol (2000) 299:255-279. DOI 10.1006/jmbi.2000.3722 · PubMed

Other PDB entries of the same protein (UniProt P09850 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8QY3 1.24 Å, Xylanase from Bacillus circulans mutant E78Q/F125A bound to xylotriose
8R85 1.3 Å, Xylanase from Bacillus circulans mutant E78Q/W9A
8QXY 1.41 Å, Xylanase from Bacillus circulans mutant E78Q bound to xylotriose
1XNB 1.49 Å, High-resolution structures of xylanases from B. Circulans and T. Harzianum identify a…
2BVV 1.5 Å, Sugar ring distortion in the glycosyl-enzyme intermediate of a family G/11 xylanase.
8QXZ 1.5 Å, Xylanase from Bacillus circulans mutant E78Q/Y69A
8R86 1.5 Å, Xylanase from Bacillus circulans mutant E78Q/W71A
3VZK 1.55 Å, Crystal structure of the Bacillus circulans endo-beta-(1,4)-xylanase (BcX) N35E mutant
1HV0 1.6 Å, Dissecting electrostatic interactions and the PH-dependent activity of a family 11…
1XNC 1.6 Å, Thermostabilization of the bacillus circulans xylanase, by the introduction of disulfide…
3VZN 1.67 Å, Crystal structure of the Bacillus circulans endo-beta-(1,4)-xylanase (BcX) N35E mutant…
8QY2 1.7 Å, Xylanase from Bacillus circulans mutant E78Q/F125A

Browse structure collections

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