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1XYS

CATALYTIC CORE OF XYLANASE A E246C MUTANT

Summary for 1XYS
Entry DOI10.2210/pdb1xys/pdb
DescriptorXYLANASE A, CALCIUM ION (2 entities in total)
Functional Keywordsfamily f xylanase, family 10 of glycosyl-hydrolase, hydrolase
Biological sourceCellvibrio japonicus
Total number of polymer chains2
Total formula weight76949.17
Authors
Harris, G.W.,Jenkins, J.A.,Connerton, I.,Pickersgill, R.W. (deposition date: 1994-09-02, release date: 1995-07-10, Last modification date: 2024-02-14)
Primary citationHarris, G.W.,Jenkins, J.A.,Connerton, I.,Cummings, N.,Lo Leggio, L.,Scott, M.,Hazlewood, G.P.,Laurie, J.I.,Gilbert, H.J.,Pickersgill, R.W.
Structure of the catalytic core of the family F xylanase from Pseudomonas fluorescens and identification of the xylopentaose-binding sites.
Structure, 2:1107-1116, 1994
Cited by
PubMed Abstract: Sequence alignment suggests that xylanases evolved from two ancestral proteins and therefore can be grouped into two families, designated F and G. Family F enzymes show no sequence similarity with any known structure and their architecture is unknown. Studies of an inactive enzyme-substrate complex will help to elucidate the structural basis of binding and catalysis in the family F xylanases.
PubMed: 7881909
DOI: 10.1016/S0969-2126(94)00112-X
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.5 Å)
Structure validation

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