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PDB: 5 results

4APE
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BU of 4ape by Molmil
THE ACTIVE SITE OF ASPARTIC PROTEINASES
Descriptor: ENDOTHIAPEPSIN
Authors:Pearl, L.H, Sewell, B.T, Jenkins, J.A, Cooper, J.B, Blundell, T.L.
Deposit date:1986-06-09
Release date:1986-07-14
Last modified:2019-10-16
Method:X-RAY DIFFRACTION (2.1 Å)
Cite:The Active Site of Aspartic Proteinases
FEBS Lett., 174, 1984
1CLX
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CATALYTIC CORE OF XYLANASE A
Descriptor: CALCIUM ION, XYLANASE A
Authors:Harris, G.W, Jenkins, J.A, Connerton, I, Pickersgill, R.W.
Deposit date:1995-08-31
Release date:1996-06-20
Last modified:2011-07-13
Method:X-RAY DIFFRACTION (1.8 Å)
Cite:Refined crystal structure of the catalytic domain of xylanase A from Pseudomonas fluorescens at 1.8 A resolution.
Acta Crystallogr.,Sect.D, 52, 1996
1XYS
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CATALYTIC CORE OF XYLANASE A E246C MUTANT
Descriptor: CALCIUM ION, XYLANASE A
Authors:Harris, G.W, Jenkins, J.A, Connerton, I, Pickersgill, R.W.
Deposit date:1994-09-02
Release date:1995-07-10
Last modified:2024-02-14
Method:X-RAY DIFFRACTION (2.5 Å)
Cite:Structure of the catalytic core of the family F xylanase from Pseudomonas fluorescens and identification of the xylopentaose-binding sites.
Structure, 2, 1994
1E5N
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E246C mutant of P fluorescens subsp. cellulosa xylanase A in complex with xylopentaose
Descriptor: CALCIUM ION, ENDO-1,4-BETA-XYLANASE A, beta-D-xylopyranose-(1-4)-beta-D-xylopyranose-(1-4)-beta-D-xylopyranose-(1-4)-beta-D-xylopyranose-(1-4)-beta-D-xylopyranose
Authors:Lo Leggio, L, Jenkins, J.A, Harris, G.W, Pickersgill, R.W.
Deposit date:2000-07-27
Release date:2000-12-08
Last modified:2023-12-13
Method:X-RAY DIFFRACTION (3.2 Å)
Cite:X-ray crystallographic study of xylopentaose binding to Pseudomonas fluorescens xylanase A.
Proteins, 41, 2000
1PCI
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PROCARICAIN
Descriptor: PROCARICAIN
Authors:Groves, M.R, Taylor, M.A.J, Scott, M, Cummings, N.J, Pickersgill, R.W, Jenkins, J.A.
Deposit date:1996-06-28
Release date:1997-04-01
Last modified:2023-08-09
Method:X-RAY DIFFRACTION (3.2 Å)
Cite:The prosequence of procaricain forms an alpha-helical domain that prevents access to the substrate-binding cleft.
Structure, 4, 1996

218853

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